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Database: UniProt
Entry: V0VJC2_ECOLX
LinkDB: V0VJC2_ECOLX
Original site: V0VJC2_ECOLX 
ID   V0VJC2_ECOLX            Unreviewed;       858 AA.
AC   V0VJC2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Penicillin-binding protein 1A {ECO:0000256|ARBA:ARBA00018638};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE            EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN   ORFNames=HMPREF1604_04065 {ECO:0000313|EMBL:ESD36038.1};
OS   Escherichia coli 908519.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=1268991 {ECO:0000313|EMBL:ESD36038.1, ECO:0000313|Proteomes:UP000017618};
RN   [1] {ECO:0000313|EMBL:ESD36038.1, ECO:0000313|Proteomes:UP000017618}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=908519 {ECO:0000313|EMBL:ESD36038.1,
RC   ECO:0000313|Proteomes:UP000017618};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA   O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA   Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00002624}.
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:0000256|ARBA:ARBA00034000};
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:0000256|ARBA:ARBA00023988};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004249}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004249}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC       family. {ECO:0000256|ARBA:ARBA00007090}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ESD36038.1}.
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DR   EMBL; AXTL01000157; ESD36038.1; -; Genomic_DNA.
DR   AlphaFoldDB; V0VJC2; -.
DR   PATRIC; fig|1268991.3.peg.3641; -.
DR   HOGENOM; CLU_006354_2_4_6; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000017618; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 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   NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF27; PENICILLIN-BINDING PROTEIN 1A; 1.
DR   Pfam; PF17092; PCB_OB; 1.
DR   Pfam; PF00912; Transgly; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          63..237
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          324..433
FT                   /note="Penicillin-binding protein OB-like"
FT                   /evidence="ECO:0000259|Pfam:PF17092"
FT   DOMAIN          437..649
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   858 AA;  94539 MW;  0D68774E4A6AFF00 CRC64;
     MKLNGKFPVK FVKYFLILAV CCILLGAGSI YGLYRYIEPQ LPDVATLKDV RLQIPMQIYS
     ADGELIAQYG EKRRIPVTLD QIPPEMVKAF IATEDSRFYE HHGVDPVGIF RAASVALFSG
     HASQGASTIT QQLARNFFLS PERTLMRKIK EVFLAIRIEQ LLTKDEILEL YLNKIYLGYR
     AYGVGAAAQV YFGKTVDQLT LNEMAVIAGL PKAPSTFNPL YSMDRAVARR NVVLSRMLDE
     GYITQQQFDQ TRTEAINANY HAPEIAFSAP YLSEMVRQEM YNRYGESAYE DGYRIYTTIT
     HKVQQAAQQA VRNNVLDYDM RHGYRGPANV LWKVGESAWD NNKITDTLKA LPTYGPLLPA
     AVTSANPQEA TAMLADGSTV VLSMEGVRWA RPYRSDTQQG PTPRKVTDVL QTGQQIWVRQ
     VDDAWWLAQV PEVNSALVSI NPQNGAVMAL VGGFDFNQSK FNRATQALRQ VGSNIKPFLY
     TAAMDKGLTL ASMLNDVPIS RWDAGAGSDW QPKNSPPQYA GPIRLRQGLG QSKNVVMVRA
     MRAMGVDYAA EYLQRFGFPA QNIVHTESLA LGSASFTPMQ VARGYAVMAN GGFLVDPWFI
     SKIENDQGGV IFEAKPKVAC PECDIPVIYG DTQKSNVLEN NDVEDVAISR EQQNVSVPMP
     QLEQANQALV AKTGAQEYAP HVINTPLAFL IKSALNTNIF GEPGWQGTGW RAGRDLQRHD
     IGGKTGTTNS SKDAWFSGYG PGVVTSVWIG FDDHRRNLGH TTASGAIKDQ ISGYEGGAKS
     AQPAWDAYMK AVLEGVPEQP LTPPPGIVTV NIDRSTGQLA NGGNSREEYF IEGTQPTQQA
     VHEVGTTIID NGEAQELF
//
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