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Putative DD-carboxypeptidase TP_0574 (EC 3.4.-.-) (47 kDa lipoprotein) (Tp47) (Tpp47) (47 kDa membrane antigen) (47-kilodalton major integral membrane immunogen)

 TA47_TREPA              Reviewed;         434 AA.
P29723; O83584;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 2.
22-NOV-2017, entry version 112.
RecName: Full=Putative DD-carboxypeptidase TP_0574 {ECO:0000303|PubMed:7972112};
EC=3.4.-.- {ECO:0000269|PubMed:7972112};
AltName: Full=47 kDa lipoprotein {ECO:0000303|PubMed:1372297};
Short=Tp47 {ECO:0000303|PubMed:12196546};
Short=Tpp47 {ECO:0000303|PubMed:7972112};
AltName: Full=47 kDa membrane antigen {ECO:0000303|PubMed:1372297};
AltName: Full=47-kilodalton major integral membrane immunogen {ECO:0000303|PubMed:9665876};
Flags: Precursor;
OrderedLocusNames=TP_0574;
Treponema pallidum (strain Nichols).
Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
NCBI_TaxID=243276;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 84-96;
126-143; 207-221; 266-298; 340-350; 366-390 AND 392-414.
STRAIN=Nichols;
PubMed=1372297;
Weigel L.M., Brandt M.E., Norgard M.V.;
"Analysis of the N-terminal region of the 47-kilodalton integral
membrane lipoprotein of Treponema pallidum.";
Infect. Immun. 60:1568-1576(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Nichols;
PubMed=9665876; DOI=10.1126/science.281.5375.375;
Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M.,
Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D.,
Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M.,
Weidman J.F., Smith H.O., Venter J.C.;
"Complete genome sequence of Treponema pallidum, the syphilis
spirochete.";
Science 281:375-388(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 68-434, AND PROTEIN SEQUENCE OF
84-96; 126-143; 207-221; 266-298; 340-350 AND 392-414.
STRAIN=Nichols;
PubMed=2642466;
Hsu P.L., Chamberlain N.R., Orth K., Moomaw C.R., Zhang L.Q.,
Slaughter C.A., Radolf J.D., Sell S., Norgard M.V.;
"Sequence analysis of the 47-kilodalton major integral membrane
immunogen of Treponema pallidum.";
Infect. Immun. 57:196-203(1989).
[4]
PENICILLIN-BINDING, AND SUBCELLULAR LOCATION.
STRAIN=Nichols;
PubMed=2647634;
Radolf J.D., Moomaw C., Slaughter C.A., Norgard M.V.;
"Penicillin-binding proteins and peptidoglycan of Treponema pallidum
subsp. pallidum.";
Infect. Immun. 57:1248-1254(1989).
[5]
PALMITOYLATION AT CYS-20, AND PROBABLE READTHROUGH.
STRAIN=Nichols;
PubMed=2668192;
Chamberlain N.R., DeOgny L., Slaughter C., Radolf J.D., Norgard M.V.;
"Acylation of the 47-kilodalton major membrane immunogen of Treponema
pallidum determines its hydrophobicity.";
Infect. Immun. 57:2878-2885(1989).
[6]
POSSIBLE FUNCTION AS A ZINC-DEPENDENT CARBOXYPEPTIDASE, AND
PENICILLIN-BINDING.
STRAIN=Nichols;
PubMed=7972112; DOI=10.1073/pnas.91.24.11611;
Weigel L.M., Radolf J.D., Norgard M.V.;
"The 47-kDa major lipoprotein immunogen of Treponema pallidum is a
penicillin-binding protein with carboxypeptidase activity.";
Proc. Natl. Acad. Sci. U.S.A. 91:11611-11615(1994).
[7]
FUNCTION IN INFECTION, SUBCELLULAR LOCATION, DIACYLGLYCEROL AT CYS-20,
AND PALMITOYLATION AT CYS-20.
PubMed=10426995; DOI=10.1126/science.285.5428.732;
Brightbill H.D., Libraty D.H., Krutzik S.R., Yang R.B., Belisle J.T.,
Bleharski J.R., Maitland M., Norgard M.V., Plevy S.E., Smale S.T.,
Brennan P.J., Bloom B.R., Godowski P.J., Modlin R.L.;
"Host defense mechanisms triggered by microbial lipoproteins through
Toll-like receptors.";
Science 285:732-736(1999).
[8]
FUNCTION IN HOST DENDRITIC CELL MATURATION.
PubMed=11160304; DOI=10.4049/jimmunol.166.4.2444;
Hertz C.J., Kiertscher S.M., Godowski P.J., Bouis D.A., Norgard M.V.,
Roth M.D., Modlin R.L.;
"Microbial lipopeptides stimulate dendritic cell maturation via Toll-
like receptor 2.";
J. Immunol. 166:2444-2450(2001).
[9] {ECO:0000244|PDB:1O75}
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 26-434, FUNCTION, SUBUNIT,
MUTAGENESIS OF 24-HIS--HIS-28; SER-119; LYS-306 AND CYS-315, AND
PENICILLIN-BINDING.
PubMed=12196546; DOI=10.1074/jbc.M207402200;
Deka R.K., Machius M., Norgard M.V., Tomchick D.R.;
"Crystal structure of the 47-kDa lipoprotein of Treponema pallidum
reveals a novel penicillin-binding protein.";
J. Biol. Chem. 277:41857-41864(2002).
-!- FUNCTION: A possible D,D-carboxypeptidase, that releases amino
acids sequentially from a proteins C-terminus (PubMed:7972112,
PubMed:12196546). Has zinc-dependent carboxypeptidase activity on
synthetic depsipeptide substrates (PubMed:7972112). May serve to
decrease cross-linking of peptidoglycan, promoting the highly
sinusous motility of this spirochaete (Probable). Overexpression
of the whole protein in E.coli leads to aberrant cell morphology
and extrusion of the cytoplasm, while overexpression of a
construct with the first 62 resides of the protein fused to PhoA
does have this effect, suggesting the whole protein, not the
lipoprotein moiety, is toxic (PubMed:7972112). Binds penicillin
(PubMed:2647634, PubMed:7972112). Penicillin binding is covalent,
does not require lipidation, and is zinc-dependent
(PubMed:7972112, PubMed:12196546). While this protein has beta-
lactamase activity in vitro, that is probably not its role in
vivo, as T.pallidum is very sensitive to penicillin antibiotics
(PubMed:12196546). {ECO:0000269|PubMed:12196546,
ECO:0000269|PubMed:2647634, ECO:0000269|PubMed:7972112,
ECO:0000305|PubMed:7972112}.
-!- FUNCTION: A pathogen-specific membrane antigen (PubMed:2642466,
PubMed:1372297). Most abundant of the membrane lipoproteins, only
found in pathogenic treponemes, suggesting that it is an important
structural moiety in the cell envelope of virulent treponemal
subspecies. A lipopeptide corresponding to the first 6 mature
residues induces host (human and mouse) cytokine release by
monocyte cell lines via TLR2 and CD14; nonlipidated protein does
not stimulate host cells (PubMed:10426995). Stimulates host
(human) dendritic cell maturation to become MHC class II-positive
antigen presenting cells via TLR2, which depends on lipidation;
nonlipidated protein does not stimulate maturation
(PubMed:11160304). {ECO:0000269|PubMed:10426995,
ECO:0000269|PubMed:11160304, ECO:0000269|PubMed:1372297,
ECO:0000269|PubMed:2642466}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:7972112};
Note=Carboxypeptidase activity is stimulated by zinc
(PubMed:7972112). Penicillin-binding is stimulated by zinc
(PubMed:12196546). {ECO:0000269|PubMed:12196546,
ECO:0000269|PubMed:7972112};
-!- SUBUNIT: Probably a monomer; a non-lipidated construct (residues
22-434) is monomeric in solution but crystallizes as a homodimer.
{ECO:0000269|PubMed:12196546}.
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000305|PubMed:7972112}; Lipid-anchor
{ECO:0000305|PubMed:10426995}.
-!- PTM: The N-terminus is blocked (PubMed:2642466). Present as a
doublet of low abundance 48 kDa and high abundance 47 kDa proteins
(PubMed:2647634, PubMed:2668192, PubMed:1372297). The longer form
is probably due to readthrough of the stop codon; the extra amino
acids at the C-terminus would be X-Lys-Arg-Gly-Val-Leu-Ser-Arg-
Val-Ser, a peptide antibody against this sequence detects only the
48 kDa form (PubMed:2668192). {ECO:0000269|PubMed:1372297,
ECO:0000269|PubMed:2642466, ECO:0000269|PubMed:2647634,
ECO:0000269|PubMed:2668192}.
-!- MISCELLANEOUS: A recombinant non-lipidated form (residues 20-434)
is recognized by human antisera, indicating the lipidation site is
not essential for antigenicity, although the acylated lipopeptide
clearly is antigenic (PubMed:1372297, PubMed:10426995). The non-
lipidated form binds also penicillin (PubMed:7972112).
{ECO:0000269|PubMed:10426995, ECO:0000269|PubMed:1372297,
ECO:0000269|PubMed:7972112}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M88769; AAA75016.1; -; Genomic_DNA.
EMBL; M88769; AAA75017.1; ALT_TERM; Genomic_DNA.
EMBL; AE000520; AAC65545.1; -; Genomic_DNA.
PIR; D71309; D71309.
RefSeq; WP_010882021.1; NC_021490.2.
PDB; 1O75; X-ray; 1.95 A; A/B=25-434.
PDBsum; 1O75; -.
ProteinModelPortal; P29723; -.
SMR; P29723; -.
STRING; 243276.TP0574; -.
EnsemblBacteria; AAC65545; AAC65545; TP_0574.
KEGG; tpa:TP_0574; -.
eggNOG; ENOG4107TXU; Bacteria.
eggNOG; ENOG410ZW1B; LUCA.
OMA; SADSWWE; -.
SABIO-RK; P29723; -.
EvolutionaryTrace; P29723; -.
Proteomes; UP000000811; Chromosome.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
GO; GO:0052157; P:modulation by symbiont of microbe-associated molecular pattern-induced host innate immune response; IDA:UniProtKB.
InterPro; IPR029221; PBP-Tp47_A.
InterPro; IPR029218; PBP-Tp47_dom_C.
InterPro; IPR036154; Tp47_N_sf.
Pfam; PF14889; PBP-Tp47_a; 1.
Pfam; PF14888; PBP-Tp47_c; 1.
SUPFAM; SSF82220; SSF82220; 1.
PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
1: Evidence at protein level;
3D-structure; Cell inner membrane; Cell membrane; Complete proteome;
Direct protein sequencing; Hydrolase; Lipoprotein; Membrane;
Palmitate; Protease; Reference proteome; Signal.
SIGNAL 1 19
CHAIN 20 434 Putative DD-carboxypeptidase TP_0574.
/FTId=PRO_0000018202.
LIPID 20 20 N-palmitoyl cysteine.
{ECO:0000305|PubMed:10426995,
ECO:0000305|PubMed:2668192}.
LIPID 20 20 S-diacylglycerol cysteine.
{ECO:0000305|PubMed:10426995}.
MUTAGEN 24 28 HHETH->SHETS: Protein still binds
ampicillin, in nonlipidated fragment
(residues 21-43), crystallized.
{ECO:0000303|PubMed:12196546}.
MUTAGEN 119 119 S->C,G: Protein still binds ampicillin
and penicillin, in nonlipidated fragment
(residues 21-43).
{ECO:0000303|PubMed:12196546}.
MUTAGEN 306 306 K->Q: Protein still binds ampicillin, in
nonlipidated fragment (residues 21-43).
{ECO:0000303|PubMed:12196546}.
MUTAGEN 315 315 C->A: Protein still binds ampicillin, in
nonlipidated fragment (residues 21-43).
{ECO:0000303|PubMed:12196546}.
CONFLICT 239 239 G -> V (in Ref. 1; AAA75016/AAA75017).
{ECO:0000305}.
STRAND 29 35 {ECO:0000244|PDB:1O75}.
HELIX 36 44 {ECO:0000244|PDB:1O75}.
HELIX 49 51 {ECO:0000244|PDB:1O75}.
STRAND 67 70 {ECO:0000244|PDB:1O75}.
STRAND 72 75 {ECO:0000244|PDB:1O75}.
HELIX 79 84 {ECO:0000244|PDB:1O75}.
TURN 85 87 {ECO:0000244|PDB:1O75}.
STRAND 88 104 {ECO:0000244|PDB:1O75}.
STRAND 110 126 {ECO:0000244|PDB:1O75}.
STRAND 128 133 {ECO:0000244|PDB:1O75}.
STRAND 139 143 {ECO:0000244|PDB:1O75}.
STRAND 155 159 {ECO:0000244|PDB:1O75}.
STRAND 162 182 {ECO:0000244|PDB:1O75}.
HELIX 183 185 {ECO:0000244|PDB:1O75}.
HELIX 186 193 {ECO:0000244|PDB:1O75}.
STRAND 208 213 {ECO:0000244|PDB:1O75}.
STRAND 231 239 {ECO:0000244|PDB:1O75}.
STRAND 247 256 {ECO:0000244|PDB:1O75}.
HELIX 264 271 {ECO:0000244|PDB:1O75}.
STRAND 274 281 {ECO:0000244|PDB:1O75}.
STRAND 293 295 {ECO:0000244|PDB:1O75}.
TURN 300 302 {ECO:0000244|PDB:1O75}.
STRAND 307 310 {ECO:0000244|PDB:1O75}.
STRAND 312 317 {ECO:0000244|PDB:1O75}.
HELIX 322 324 {ECO:0000244|PDB:1O75}.
STRAND 329 338 {ECO:0000244|PDB:1O75}.
STRAND 344 350 {ECO:0000244|PDB:1O75}.
STRAND 359 372 {ECO:0000244|PDB:1O75}.
TURN 374 379 {ECO:0000244|PDB:1O75}.
STRAND 380 386 {ECO:0000244|PDB:1O75}.
STRAND 392 398 {ECO:0000244|PDB:1O75}.
STRAND 400 409 {ECO:0000244|PDB:1O75}.
STRAND 414 420 {ECO:0000244|PDB:1O75}.
STRAND 422 424 {ECO:0000244|PDB:1O75}.
STRAND 427 432 {ECO:0000244|PDB:1O75}.
SEQUENCE 434 AA; 47665 MW; B5C2A75D4A8849E0 CRC64;
MKVKYALLSA GALQLLVVGC GSSHHETHYG YATLSYADYW AGELGQSRDV LLAGNAEADR
AGDLDAGMFD AVSRATHGHG AFRQQFQYAV EVLGEKVLSK QETEDSRGRK KWEYETDPSV
TKMVRASASF QDLGEDGEIK FEAVEGAVAL ADRASSFMVD SEEYKITNVK VHGMKFVPVA
VPHELKGIAK EKFHFVEDSR VTENTNGLKT MLTEDSFSAR KVSSMESPHD LVVDTVGTGY
HSRFGSDAEA SVMLKRADGS ELSHREFIDY VMNFNTVRYD YYGDDASYTN LMASYGTKHS
ADSWWKTGRV PRISCGINYG FDRFKGSGPG YYRLTLIANG YRDVVADVRF LPKYEGNIDI
GLKGKVLTIG GADAETLMDA AVDVFADGQP KLVSDQAVSL GQNVLSADFT PGTEYTVEVR
FKEFGSVRAK VVAQ


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