ID   PBPA_MYCTO              Reviewed;         491 AA.
AC   P9WKD0; L0T427; P71586; Q7DAK5;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Peptidoglycan D,D-transpeptidase PbpA {ECO:0000250|UniProtKB:P9WKD1};
DE            EC=3.4.16.4 {ECO:0000250|UniProtKB:P9WKD1};
DE   AltName: Full=Penicillin-binding protein A {ECO:0000250|UniProtKB:P9WKD1};
DE            Short=PBPA {ECO:0000250|UniProtKB:P9WKD1};
GN   Name=pbpA; OrderedLocusNames=MT0019;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Transpeptidase that catalyzes cross-linking of the
CC       peptidoglycan cell wall. Required for the regulation of cell length.
CC       {ECO:0000250|UniProtKB:P9WKD1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC         transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC         substituents of D-alanine.; EC=3.4.16.4;
CC         Evidence={ECO:0000250|UniProtKB:P9WKD1};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000250|UniProtKB:P9WKD1}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P9WKD1}; Single-pass type II membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK44241.1; -; Genomic_DNA.
DR   PIR; F70699; F70699.
DR   RefSeq; WP_003899775.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WKD0; -.
DR   SMR; P9WKD0; -.
DR   EnsemblBacteria; AAK44241; AAK44241; MT0019.
DR   GeneID; 45423975; -.
DR   KEGG; mtc:MT0019; -.
DR   PATRIC; fig|83331.31.peg.20; -.
DR   HOGENOM; CLU_009289_1_0_11; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; -; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Hydrolase; Membrane;
KW   Peptidoglycan synthesis; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..491
FT                   /note="Peptidoglycan D,D-transpeptidase PbpA"
FT                   /id="PRO_0000427675"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        8..28
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..491
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          160..484
FT                   /note="Transpeptidase"
FT   ACT_SITE        222
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AD65"
SQ   SEQUENCE   491 AA;  51576 MW;  888DBA26BE251581 CRC64;
     MNASLRRISV TVMALIVLLL LNATMTQVFT ADGLRADPRN QRVLLDEYSR QRGQITAGGQ
     LLAYSVATDG RFRFLRVYPN PEVYAPVTGF YSLRYSSTAL ERAEDPILNG SDRRLFGRRL
     ADFFTGRDPR GGNVDTTINP RIQQAGWDAM QQGCYGPCKG AVVALEPSTG KILALVSSPS
     YDPNLLASHN PEVQAQAWQR LGDNPASPLT NRAISETYPP GSTFKVITTA AALAAGATET
     EQLTAAPTIP LPGSTAQLEN YGGAPCGDEP TVSLREAFVK SCNTAFVQLG IRTGADALRS
     MARAFGLDSP PRPTPLQVAE STVGPIPDSA ALGMTSIGQK DVALTPLANA EIAATIANGG
     ITMRPYLVGS LKGPDLANIS TTVGYQQRRA VSPQVAAKLT ELMVGAEKVA QQKGAIPGVQ
     IASKTGTAEH GTDPRHTPPH AWYIAFAPAQ APKVAVAVLV ENGADRLSAT GGALAAPIGR
     AVIEAALQGE P