PBPA_MYCS2
ID PBPA_MYCS2 Reviewed; 491 AA.
AC A0QNG3; I7G139;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=MSMEG_0031, MSMEI_0033;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP RETRACTED PAPER.
RX PubMed=16436437; DOI=10.1099/mic.0.28630-0;
RA Dasgupta A., Datta P., Kundu M., Basu J.;
RT "The serine/threonine kinase PknB of Mycobacterium tuberculosis
RT phosphorylates PBPA, a penicillin-binding protein required for cell
RT division.";
RL Microbiology 152:493-504(2006).
RN [5]
RP RETRACTION NOTICE OF PUBMED:16436437.
RX PubMed=26231854; DOI=10.1099/mic.0.000110;
RA Dasgupta A., Datta P., Kundu M., Basu J.;
RL Microbiology 161:1537-1537(2015).
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; CP000480; ABK71213.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP36516.1; -; Genomic_DNA.
DR RefSeq; WP_003891359.1; NZ_SIJM01000001.1.
DR RefSeq; YP_884451.1; NC_008596.1.
DR AlphaFoldDB; A0QNG3; -.
DR SMR; A0QNG3; -.
DR STRING; 246196.MSMEI_0033; -.
DR PRIDE; A0QNG3; -.
DR EnsemblBacteria; ABK71213; ABK71213; MSMEG_0031.
DR EnsemblBacteria; AFP36516; AFP36516; MSMEI_0033.
DR GeneID; 66738222; -.
DR KEGG; msg:MSMEI_0033; -.
DR KEGG; msm:MSMEG_0031; -.
DR PATRIC; fig|246196.19.peg.29; -.
DR eggNOG; COG0768; Bacteria.
DR OMA; MWAPVTG; -.
DR OrthoDB; 423699at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..491
FT /note="Peptidoglycan D,D-transpeptidase PbpA"
FT /id="PRO_0000343833"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 9..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..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; 51332 MW; CCBF965E65CFF904 CRC64;
MNTSLRRVAV AIMVLIVLLL ANATVTQVFA ADGLRADPRN QRVLLDEYSR QRGQITAGGQ
LLAYSVSTDG RFRYLRVYPN PQAYAPVTGF YSLGYSSTGL ERAEDAVLNG SDERLFGRRL
ADFFTGRDPR GGNVDTTIKP QVQQAAWDAM QNGCDGPCRG SVVALEPSTG KILAMVSAPS
YDPNLLATHD LAAQADAWEK LRDDPQSPLL NRAISETYPP GSTFKVITTA AALQAGARPQ
TQLTSAPRTP LPDSTATLEN FGGAPCGPGP TVSLQEAFAK SCNTAFVELG LSTGTDKLKA
MAQAFGLDTP PPAIPLQVAE STTGPIVDAA ALGMSSIGQR DVALTPLQNA QVAATIANDG
IAMRPYLVES LKGPDLATIS TTTPEQERRA VSPQVAATLT DLMVAAEQVT QQKGAIAGVQ
IASKTGTAEH GTDPRNTPPH AWYIAFAPAQ DPKVAVAVLV EDGGDRLSAT GGALAAPIGR
ATIAAALREG S
