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Periplasmic zinc-binding protein TroA (Tromp-1)

 TROA_TREPA              Reviewed;         308 AA.
P96116; Q56329;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
22-NOV-2017, entry version 127.
RecName: Full=Periplasmic zinc-binding protein TroA;
AltName: Full=Tromp-1;
Flags: Precursor;
Name=troA; Synonyms=troMP1; OrderedLocusNames=TP_0163;
Treponema pallidum (strain Nichols).
Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
NCBI_TaxID=243276;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Nichols;
PubMed=7768866; DOI=10.1128/jb.177.12.3556-3562.1995;
Blanco D.R., Champion C.I., Exner M.M., Erdjument-Bromage H.,
Hancock R.E., Tempst P., Miller J.N., Lovett M.A.;
"Porin activity and sequence analysis of a 31-kilodalton Treponema
pallidum subsp. pallidum rare outer membrane protein (Tromp1).";
J. Bacteriol. 177:3556-3562(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Nichols;
PubMed=9332349; DOI=10.1016/S0378-1119(97)00234-5;
Hardham J.M., Stamm L.V., Porcella S.F., Frye J.G., Barnes N.Y.,
Howell J.K., Mueller S.L., Radolf J.D., Weinstock G.M., Norris S.J.;
"Identification and transcriptional analysis of a Treponema pallidum
operon encoding a putative ABC transport system, an iron-activated
repressor protein homolog, and a glycolytic pathway enzyme homolog.";
Gene 197:47-64(1997).
[3]
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).
[4]
CHARACTERIZATION.
PubMed=10400603;
Deka R.K., Lee Y.-H., Hagman K.E., Shevchenko D., Lingwood C.A.,
Hasemann C.A., Norgard M.V., Radolf J.D.;
"Physicochemical evidence that Treponema pallidum TroA is a zinc-
containing metalloprotein that lacks porin-like structure.";
J. Bacteriol. 181:4420-4423(1999).
[5]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 23-313.
PubMed=10404217; DOI=10.1038/10677;
Lee Y.-H., Deka R.K., Norgard M.V., Radolf J.D., Hasemann C.A.;
"Treponema pallidum TroA is a periplasmic zinc-binding protein with a
helical backbone.";
Nat. Struct. Biol. 6:628-633(1999).
-!- FUNCTION: Part of an ATP-driven transport system TroABCD for zinc.
Substrate-binding protein involved in the transport of zinc across
the cytoplasmic membrane.
-!- SUBUNIT: Monomer.
-!- SUBCELLULAR LOCATION: Periplasm.
-!- SIMILARITY: Belongs to the bacterial solute-binding protein 9
family. {ECO:0000305}.
-!- CAUTION: Was originally thought to be an outer membrane protein
with porin-like properties. {ECO:0000305|PubMed:7768866}.
-!- SEQUENCE CAUTION:
Sequence=AAA92353.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U16363; AAA92353.1; ALT_INIT; Genomic_DNA.
EMBL; U55214; AAC45725.1; -; Genomic_DNA.
EMBL; AE000520; AAC65151.1; -; Genomic_DNA.
PIR; A71360; A71360.
RefSeq; WP_010881610.1; NC_021490.2.
PDB; 1K0F; X-ray; 2.50 A; A=32-308.
PDB; 1TOA; X-ray; 1.80 A; A/B=23-308.
PDBsum; 1K0F; -.
PDBsum; 1TOA; -.
ProteinModelPortal; P96116; -.
SMR; P96116; -.
IntAct; P96116; 8.
STRING; 243276.TP0163; -.
TCDB; 3.A.1.15.8; the atp-binding cassette (abc) superfamily.
EnsemblBacteria; AAC65151; AAC65151; TP_0163.
GeneID; 34332142; -.
KEGG; tpa:TP_0163; -.
eggNOG; ENOG4107SIG; Bacteria.
eggNOG; COG0803; LUCA.
KO; K11707; -.
OMA; DPHIWFD; -.
EvolutionaryTrace; P96116; -.
Proteomes; UP000000811; Chromosome.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IEA:InterPro.
GO; GO:0006829; P:zinc II ion transport; IEA:UniProtKB-KW.
InterPro; IPR006129; AdhesinB.
InterPro; IPR006128; Lipoprotein_4.
InterPro; IPR006127; ZnuA-like.
Pfam; PF01297; ZnuA; 1.
PRINTS; PR00691; ADHESINB.
PRINTS; PR00690; ADHESNFAMILY.
1: Evidence at protein level;
3D-structure; Complete proteome; Ion transport; Metal-binding;
Periplasm; Reference proteome; Signal; Transport; Zinc;
Zinc transport.
SIGNAL 1 22
CHAIN 23 308 Periplasmic zinc-binding protein TroA.
/FTId=PRO_0000031872.
METAL 68 68 Zinc.
METAL 133 133 Zinc.
METAL 199 199 Zinc.
METAL 279 279 Zinc.
STRAND 35 40 {ECO:0000244|PDB:1TOA}.
HELIX 41 51 {ECO:0000244|PDB:1TOA}.
HELIX 52 54 {ECO:0000244|PDB:1TOA}.
STRAND 55 60 {ECO:0000244|PDB:1TOA}.
TURN 67 69 {ECO:0000244|PDB:1TOA}.
HELIX 74 82 {ECO:0000244|PDB:1TOA}.
STRAND 84 88 {ECO:0000244|PDB:1TOA}.
TURN 91 94 {ECO:0000244|PDB:1K0F}.
HELIX 95 97 {ECO:0000244|PDB:1K0F}.
HELIX 98 104 {ECO:0000244|PDB:1TOA}.
STRAND 107 112 {ECO:0000244|PDB:1TOA}.
HELIX 113 116 {ECO:0000244|PDB:1TOA}.
HELIX 119 121 {ECO:0000244|PDB:1TOA}.
TURN 126 128 {ECO:0000244|PDB:1K0F}.
HELIX 134 136 {ECO:0000244|PDB:1TOA}.
HELIX 138 155 {ECO:0000244|PDB:1TOA}.
HELIX 157 159 {ECO:0000244|PDB:1TOA}.
HELIX 160 186 {ECO:0000244|PDB:1TOA}.
HELIX 190 192 {ECO:0000244|PDB:1TOA}.
STRAND 194 200 {ECO:0000244|PDB:1TOA}.
HELIX 203 209 {ECO:0000244|PDB:1TOA}.
STRAND 212 217 {ECO:0000244|PDB:1TOA}.
STRAND 221 223 {ECO:0000244|PDB:1K0F}.
HELIX 227 239 {ECO:0000244|PDB:1TOA}.
STRAND 243 248 {ECO:0000244|PDB:1TOA}.
HELIX 254 264 {ECO:0000244|PDB:1TOA}.
TURN 265 267 {ECO:0000244|PDB:1TOA}.
STRAND 271 276 {ECO:0000244|PDB:1TOA}.
STRAND 278 280 {ECO:0000244|PDB:1TOA}.
HELIX 287 289 {ECO:0000244|PDB:1TOA}.
HELIX 291 306 {ECO:0000244|PDB:1TOA}.
SEQUENCE 308 AA; 33570 MW; 2FDD8FF20D012B08 CRC64;
MIRERICACV LALGMLTGFT HAFGSKDAAA DGKPLVVTTI GMIADAVKNI AQGDVHLKGL
MGPGVDPHLY TATAGDVEWL GNADLILYNG LHLETKMGEV FSKLRGSRLV VAVSETIPVS
QRLSLEEAEF DPHVWFDVKL WSYSVKAVYE SLCKLLPGKT REFTQRYQAY QQQLDKLDAY
VRRKAQSLPA ERRVLVTAHD AFGYFSRAYG FEVKGLQGVS TASEASAHDM QELAAFIAQR
KLPAIFIESS IPHKNVEALR DAVQARGHVV QIGGELFSDA MGDAGTSEGT YVGMVTHNID
TIVAALAR


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