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Penicillin-binding protein 1A (PBP-1A) (Penicillin-binding protein 1*) [Includes: Penicillin-insensitive transglycosylase (EC 2.4.1.129) (Peptidoglycan TGase); Penicillin-sensitive transpeptidase (EC 3.4.16.4) (DD-transpeptidase)]

 PBP1A_MYCTU             Reviewed;         820 AA.
P71707; L0T5D2;
06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
06-FEB-2013, sequence version 3.
23-MAY-2018, entry version 100.
RecName: Full=Penicillin-binding protein 1A;
Short=PBP-1A;
AltName: Full=Penicillin-binding protein 1*;
Includes:
RecName: Full=Penicillin-insensitive transglycosylase;
EC=2.4.1.129 {ECO:0000250|UniProtKB:P02918};
AltName: Full=Peptidoglycan TGase;
Includes:
RecName: Full=Penicillin-sensitive transpeptidase;
EC=3.4.16.4 {ECO:0000250|UniProtKB:P02918};
AltName: Full=DD-transpeptidase;
Name=ponA1; OrderedLocusNames=Rv0050; ORFNames=MTCY21D4.13;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
PENICILLIN-BINDING.
STRAIN=ATCC 25618 / H37Rv;
PubMed=11802794; DOI=10.1042/0264-6021:3610635;
Bhakta S., Basu J.;
"Overexpression, purification and biochemical characterization of a
class A high-molecular-mass penicillin-binding protein (PBP), PBP1*
and its soluble derivative from Mycobacterium tuberculosis.";
Biochem. J. 361:635-639(2002).
[3]
FUNCTION, INTERACTION WITH RIPA, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 25618 / H37Rv;
PubMed=20686708; DOI=10.1371/journal.ppat.1001020;
Hett E.C., Chao M.C., Rubin E.J.;
"Interaction and modulation of two antagonistic cell wall enzymes of
mycobacteria.";
PLoS Pathog. 6:E1001020-E1001020(2010).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
-!- FUNCTION: Cell wall formation. Synthesis of cross-linked
peptidoglycan from the lipid intermediates. The enzyme has a
penicillin-insensitive transglycosylase N-terminal domain
(formation of linear glycan strands) and a penicillin-sensitive
transpeptidase C-terminal domain (cross-linking of the peptide
subunits) (By similarity). Has little peptidoglycan hydrolytic
activity; however it inhibits the synergistic peptidoglycan
hydrolysis of RipA plus RpfB. {ECO:0000250,
ECO:0000269|PubMed:20686708}.
-!- CATALYTIC ACTIVITY: (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-
Lys-D-Ala-D-Ala))(n)-diphosphoundecaprenol + GlcNAc-(1->4)-
Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-
Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl
diphosphate. {ECO:0000250|UniProtKB:P02918}.
-!- CATALYTIC ACTIVITY: Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-
D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are
N-acyl substituents of D-alanine. {ECO:0000250|UniProtKB:P02918}.
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
-!- SUBUNIT: Interacts with RipA via its transpeptidase domain
(residues 561-820). {ECO:0000269|PubMed:20686708}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
membrane protein {ECO:0000305}. Note=Localizes to poles and
occasionally septa upon expression in M.smegmatis.
{ECO:0000269|PubMed:20686708}.
-!- DOMAIN: A penicillin-binding domain is found between residues 420-
820.
-!- SIMILARITY: In the N-terminal section; belongs to the
glycosyltransferase 51 family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the
transpeptidase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CCP42772.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AL123456; CCP42772.1; ALT_INIT; Genomic_DNA.
PIR; B70913; B70913.
RefSeq; YP_177687.1; NC_000962.3.
PDB; 5CRF; X-ray; 1.80 A; A/B/C/D=391-820.
PDB; 5CXW; X-ray; 1.75 A; A=391-820.
PDBsum; 5CRF; -.
PDBsum; 5CXW; -.
ProteinModelPortal; P71707; -.
SMR; P71707; -.
STRING; 83332.Rv0050; -.
CAZy; GT51; Glycosyltransferase Family 51.
PaxDb; P71707; -.
EnsemblBacteria; CCP42772; CCP42772; Rv0050.
GeneID; 887065; -.
KEGG; mtu:Rv0050; -.
PATRIC; fig|83332.12.peg.56; -.
TubercuList; Rv0050; -.
eggNOG; ENOG4105BZ4; Bacteria.
eggNOG; COG0744; LUCA.
HOGENOM; HOG000041137; -.
InParanoid; P71707; -.
UniPathway; UPA00219; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:MTBBASE.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0008658; F:penicillin binding; IDA:MTBBASE.
GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0071456; P:cellular response to hypoxia; IEP:MTBBASE.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
Gene3D; 1.10.3810.10; -; 1.
InterPro; IPR012338; Beta-lactam/transpept-like.
InterPro; IPR001264; Glyco_trans_51.
InterPro; IPR023346; Lysozyme-like_dom_sf.
InterPro; IPR036950; PBP_transglycosylase.
InterPro; IPR001460; PCN-bd_Tpept.
Pfam; PF00912; Transgly; 1.
Pfam; PF00905; Transpeptidase; 1.
SUPFAM; SSF53955; SSF53955; 1.
SUPFAM; SSF56601; SSF56601; 2.
1: Evidence at protein level;
3D-structure; Carboxypeptidase; Cell membrane; Cell shape;
Cell wall biogenesis/degradation; Complete proteome;
Glycosyltransferase; Hydrolase; Membrane; Multifunctional enzyme;
Peptidoglycan synthesis; Protease; Reference proteome; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 820 Penicillin-binding protein 1A.
/FTId=PRO_0000421124.
TRANSMEM 139 159 Helical. {ECO:0000255}.
REGION 180 360 Transglycosylase.
REGION 453 743 Transpeptidase.
COMPBIAS 63 123 Pro-rich.
COMPBIAS 767 820 Pro-rich.
ACT_SITE 213 213 Proton donor; for transglycosylase
activity. {ECO:0000250|UniProtKB:P02919}.
ACT_SITE 487 487 Acyl-ester intermediate; for
transpeptidase activity.
{ECO:0000250|UniProtKB:P02919}.
HELIX 392 409 {ECO:0000244|PDB:5CXW}.
HELIX 413 419 {ECO:0000244|PDB:5CXW}.
STRAND 422 425 {ECO:0000244|PDB:5CXW}.
HELIX 429 443 {ECO:0000244|PDB:5CXW}.
STRAND 450 457 {ECO:0000244|PDB:5CXW}.
TURN 459 461 {ECO:0000244|PDB:5CXW}.
STRAND 463 468 {ECO:0000244|PDB:5CXW}.
HELIX 486 489 {ECO:0000244|PDB:5CXW}.
HELIX 490 499 {ECO:0000244|PDB:5CXW}.
STRAND 507 509 {ECO:0000244|PDB:5CXW}.
STRAND 513 515 {ECO:0000244|PDB:5CXW}.
STRAND 518 520 {ECO:0000244|PDB:5CXW}.
HELIX 523 525 {ECO:0000244|PDB:5CXW}.
STRAND 529 532 {ECO:0000244|PDB:5CXW}.
HELIX 533 539 {ECO:0000244|PDB:5CXW}.
HELIX 542 551 {ECO:0000244|PDB:5CXW}.
HELIX 555 566 {ECO:0000244|PDB:5CXW}.
STRAND 575 577 {ECO:0000244|PDB:5CXW}.
STRAND 583 585 {ECO:0000244|PDB:5CXW}.
HELIX 590 594 {ECO:0000244|PDB:5CXW}.
STRAND 597 599 {ECO:0000244|PDB:5CXW}.
HELIX 601 612 {ECO:0000244|PDB:5CXW}.
TURN 613 615 {ECO:0000244|PDB:5CXW}.
STRAND 621 627 {ECO:0000244|PDB:5CXW}.
STRAND 633 636 {ECO:0000244|PDB:5CXW}.
TURN 637 639 {ECO:0000244|PDB:5CRF}.
HELIX 650 660 {ECO:0000244|PDB:5CXW}.
HELIX 663 666 {ECO:0000244|PDB:5CXW}.
HELIX 673 675 {ECO:0000244|PDB:5CXW}.
STRAND 679 686 {ECO:0000244|PDB:5CXW}.
STRAND 690 702 {ECO:0000244|PDB:5CXW}.
STRAND 705 716 {ECO:0000244|PDB:5CXW}.
TURN 730 732 {ECO:0000244|PDB:5CXW}.
HELIX 733 746 {ECO:0000244|PDB:5CXW}.
STRAND 763 766 {ECO:0000244|PDB:5CXW}.
SEQUENCE 820 AA; 85969 MW; 6DD7A149081D3EB4 CRC64;
MNSDGRHHQS SSGAPRGPAN PGQRGQVPPD DRLTAILPPV TDDRSAPHAD SIEAVKAALD
GAPPMPPPRD PLEEVTAALA APPGKPPRGD QLGGRRRPPG PPGPPGSSGQ PAGRLPQPRV
DLPRVGQINW KWIRRSLYLT AAVVILLPMV TFTMAYLIVD VPKPGDIRTN QVSTILASDG
SEIAKIVPPE GNRVDVNLSQ VPMHVRQAVI AAEDRNFYSN PGFSFTGFAR AVKNNLFGGD
LQGGSTITQQ YVKNALVGSA QHGWSGLMRK AKELVIATKM SGEWSKDDVL QAYLNIIYFG
RGAYGISAAS KAYFDKPVEQ LTVAEGALLA ALIRRPSTLD PAVDPEGAHA RWNWVLDGMV
ETKALSPNDR AAQVFPETVP PDLARAENQT KGPNGLIERQ VTRELLELFN IDEQTLNTQG
LVVTTTIDPQ AQRAAEKAVA KYLDGQDPDM RAAVVSIDPH NGAVRAYYGG DNANGFDFAQ
AGLQTGSSFK VFALVAALEQ GIGLGYQVDS SPLTVDGIKI TNVEGEGCGT CNIAEALKMS
LNTSYYRLML KLNGGPQAVA DAAHQAGIAS SFPGVAHTLS EDGKGGPPNN GIVLGQYQTR
VIDMASAYAT LAASGIYHPP HFVQKVVSAN GQVLFDASTA DNTGDQRIPK AVADNVTAAM
EPIAGYSRGH NLAGGRDSAA KTGTTQFGDT TANKDAWMVG YTPSLSTAVW VGTVKGDEPL
VTASGAAIYG SGLPSDIWKA TMDGALKGTS NETFPKPTEV GGYAGVPPPP PPPEVPPSET
VIQPTVEIAP GITIPIGPPT TITLAPPPPA PPAATPTPPP


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