PBPA_ECOLI
ID PBPA_ECOLI Reviewed; 850 AA.
AC P02918; P76688; Q2M761;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Penicillin-binding protein 1A;
DE Short=PBP-1a;
DE Short=PBP1a;
DE Includes:
DE RecName: Full=Penicillin-insensitive transglycosylase;
DE EC=2.4.1.129 {ECO:0000269|PubMed:7006606};
DE AltName: Full=Peptidoglycan TGase;
DE Includes:
DE RecName: Full=Penicillin-sensitive transpeptidase;
DE EC=3.4.16.4 {ECO:0000269|PubMed:7006606};
DE AltName: Full=DD-transpeptidase;
GN Name=mrcA; Synonyms=ponA; OrderedLocusNames=b3396, JW3359;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3882429; DOI=10.1111/j.1432-1033.1985.tb08768.x;
RA Broome-Smith J.K., Edelman A., Yousif S., Spratt B.G.;
RT "The nucleotide sequences of the ponA and ponB genes encoding penicillin-
RT binding protein 1A and 1B of Escherichia coli K12.";
RL Eur. J. Biochem. 147:437-446(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROTEIN SEQUENCE OF 452-480.
RC STRAIN=K12;
RX PubMed=3920658; DOI=10.1073/pnas.82.7.1999;
RA Keck W., Glauner B., Schwarz U., Broome-Smith J.K., Spratt B.G.;
RT "Sequences of the active-site peptides of three of the high-Mr penicillin-
RT binding proteins of Escherichia coli K-12.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:1999-2003(1985).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=7006606; DOI=10.1016/s0006-291x(80)80166-5;
RA Ishino F., Mitsui K., Tamaki S., Matsuhashi M.;
RT "Dual enzyme activities of cell wall peptidoglycan synthesis, peptidoglycan
RT transglycosylase and penicillin-sensitive transpeptidase, in purified
RT preparations of Escherichia coli penicillin-binding protein 1A.";
RL Biochem. Biophys. Res. Commun. 97:287-293(1980).
RN [6]
RP REVIEW.
RX PubMed=9841666; DOI=10.1128/mmbr.62.4.1079-1093.1998;
RA Goffin C., Ghuysen J.-M.;
RT "Multimodular penicillin-binding proteins: an enigmatic family of orthologs
RT and paralogs.";
RL Microbiol. Mol. Biol. Rev. 62:1079-1093(1998).
CC -!- FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan
CC from the lipid intermediates. The enzyme has a penicillin-insensitive
CC transglycosylase N-terminal domain (formation of linear glycan strands)
CC and a penicillin-sensitive transpeptidase C-terminal domain (cross-
CC linking of the peptide subunits). {ECO:0000269|PubMed:7006606}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129;
CC Evidence={ECO:0000269|PubMed:7006606};
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:0000269|PubMed:7006606};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000269|PubMed:7006606}.
CC -!- INTERACTION:
CC P02918; P45464: lpoA; NbExp=4; IntAct=EBI-1126191, EBI-557795;
CC P02918; P0AD65: mrdA; NbExp=5; IntAct=EBI-1126191, EBI-1124032;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:7006606};
CC Single-pass type II membrane protein {ECO:0000255}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58193.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X02164; CAA26100.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58193.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76421.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77895.1; -; Genomic_DNA.
DR PIR; G65134; ZPECPA.
DR RefSeq; NP_417855.4; NC_000913.3.
DR RefSeq; WP_001336003.1; NZ_SSZK01000008.1.
DR AlphaFoldDB; P02918; -.
DR SMR; P02918; -.
DR BioGRID; 4262992; 302.
DR ComplexPortal; CPX-5718; Elongasome complex.
DR DIP; DIP-10251N; -.
DR IntAct; P02918; 9.
DR STRING; 511145.b3396; -.
DR ChEMBL; CHEMBL1813; -.
DR DrugBank; DB01602; Bacampicillin.
DR DrugBank; DB00578; Carbenicillin.
DR DrugBank; DB09319; Carindacillin.
DR DrugBank; DB01414; Cefacetrile.
DR DrugBank; DB01327; Cefazolin.
DR DrugBank; DB00274; Cefmetazole.
DR DrugBank; DB01328; Cefonicid.
DR DrugBank; DB01329; Cefoperazone.
DR DrugBank; DB01331; Cefoxitin.
DR DrugBank; DB00430; Cefpiramide.
DR DrugBank; DB01333; Cefradine.
DR DrugBank; DB00438; Ceftazidime.
DR DrugBank; DB01415; Ceftibuten.
DR DrugBank; DB01332; Ceftizoxime.
DR DrugBank; DB09050; Ceftolozane.
DR DrugBank; DB01000; Cyclacillin.
DR DrugBank; DB06211; Doripenem.
DR DrugBank; DB00303; Ertapenem.
DR DrugBank; DB01598; Imipenem.
DR DrugBank; DB04570; Latamoxef.
DR DrugCentral; P02918; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR jPOST; P02918; -.
DR PaxDb; P02918; -.
DR PRIDE; P02918; -.
DR EnsemblBacteria; AAC76421; AAC76421; b3396.
DR EnsemblBacteria; BAE77895; BAE77895; BAE77895.
DR GeneID; 947907; -.
DR KEGG; ecj:JW3359; -.
DR KEGG; eco:b3396; -.
DR PATRIC; fig|1411691.4.peg.3334; -.
DR EchoBASE; EB0741; -.
DR eggNOG; COG5009; Bacteria.
DR HOGENOM; CLU_006354_2_4_6; -.
DR InParanoid; P02918; -.
DR OMA; LAQMAMI; -.
DR PhylomeDB; P02918; -.
DR BioCyc; EcoCyc:EG10748-MON; -.
DR BioCyc; MetaCyc:EG10748-MON; -.
DR UniPathway; UPA00219; -.
DR PRO; PR:P02918; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0008658; F:penicillin binding; IDA:EcoCyc.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IDA:EcoCyc.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IDA:EcoCyc.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IDA:EcoCyc.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IC:ComplexPortal.
DR GO; GO:0046677; P:response to antibiotic; IDA:EcoCyc.
DR Gene3D; 1.10.3810.10; -; 1.
DR Gene3D; 3.40.710.10; -; 2.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR031376; PCB_OB.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR Pfam; PF17092; PCB_OB; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Carboxypeptidase; Cell inner membrane;
KW Cell membrane; Cell shape; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Glycosyltransferase; Hydrolase; Membrane;
KW Multifunctional enzyme; Peptidoglycan synthesis; Protease;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..850
FT /note="Penicillin-binding protein 1A"
FT /id="PRO_0000083164"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..850
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT REGION 48..216
FT /note="Transglycosylase"
FT REGION 400..710
FT /note="Transpeptidase"
FT ACT_SITE 86
FT /note="Proton donor; for transglycosylase activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT ACT_SITE 465
FT /note="Acyl-ester intermediate; for transpeptidase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
SQ SEQUENCE 850 AA; 93636 MW; 0A54C6B28783E34B CRC64;
MKFVKYFLIL AVCCILLGAG SIYGLYRYIE PQLPDVATLK DVRLQIPMQI YSADGELIAQ
YGEKRRIPVT LDQIPPEMVK AFIATEDSRF YEHHGVDPVG IFRAASVALF SGHASQGAST
ITQQLARNFF LSPERTLMRK IKEVFLAIRI EQLLTKDEIL ELYLNKIYLG YRAYGVGAAA
QVYFGKTVDQ LTLNEMAVIA GLPKAPSTFN PLYSMDRAVA RRNVVLSRML DEGYITQQQF
DQTRTEAINA NYHAPEIAFS APYLSEMVRQ EMYNRYGESA YEDGYRIYTT ITRKVQQAAQ
QAVRNNVLDY DMRHGYRGPA NVLWKVGESA WDNNKITDTL KALPTYGPLL PAAVTSANPQ
QATAMLADGS TVALSMEGVR WARPYRSDTQ QGPTPRKVTD VLQTGQQIWV RQVGDAWWLA
QVPEVNSALV SINPQNGAVM ALVGGFDFNQ SKFNRATQAL RQVGSNIKPF LYTAAMDKGL
TLASMLNDVP ISRWDASAGS DWQPKNSPPQ YAGPIRLRQG LGQSKNVVMV RAMRAMGVDY
AAEYLQRFGF PAQNIVHTES LALGSASFTP MQVARGYAVM ANGGFLVDPW FISKIENDQG
GVIFEAKPKV ACPECDIPVI YGDTQKSNVL ENNDVEDVAI SREQQNVSVP MPQLEQANQA
LVAKTGAQEY APHVINTPLA FLIKSALNTN IFGEPGWQGT GWRAGRDLQR RDIGGKTGTT
NSSKDAWFSG YGPGVVTSVW IGFDDHRRNL GHTTASGAIK DQISGYEGGA KSAQPAWDAY
MKAVLEGVPE QPLTPPPGIV TVNIDRSTGQ LANGGNSREE YFIEGTQPTQ QAVHEVGTTI
IDNGEAQELF
