ID Q8X809_ECO57 Unreviewed; 850 AA.
AC Q8X809; A0A6M0JFM0; Q7AAB9;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 2.
DT 27-MAR-2024, entry version 152.
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 Name=mrcA {ECO:0000313|EMBL:BAB37661.2};
GN ORFNames=ECs_4238 {ECO:0000313|EMBL:BAB37661.2};
OS Escherichia coli O157:H7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB37661.2, ECO:0000313|Proteomes:UP000000558};
RN [1] {ECO:0000313|EMBL:BAB37661.2, ECO:0000313|Proteomes:UP000000558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC
RC {ECO:0000313|Proteomes:UP000000558};
RX PubMed=11258796; DOI=.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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}.
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DR EMBL; BA000007; BAB37661.2; -; Genomic_DNA.
DR RefSeq; NP_312265.2; NC_002695.1.
DR RefSeq; WP_001301905.1; NZ_VOAI01000004.1.
DR AlphaFoldDB; Q8X809; -.
DR STRING; 155864.Z4750; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR GeneID; 75173553; -.
DR GeneID; 915905; -.
DR KEGG; ecs:ECs_4238; -.
DR PATRIC; fig|386585.9.peg.4424; -.
DR eggNOG; COG5009; Bacteria.
DR HOGENOM; CLU_006354_2_4_6; -.
DR OMA; LAQMAMI; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000558; Chromosome.
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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000000558};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT DOMAIN 55..229
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 316..425
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 429..641
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 850 AA; 93607 MW; B468A0F0E3A2CD52 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
EATAMLADGS TVALSMEGVR WARPYRSDTQ QGPTPRKVTD VLQTGQQIWV RQVGDAWWLA
QVPEVNSALV SINPQNGAVM ALVGGFDFNQ SKFNRATQAL RQVGSNIKPF LYTAAMDKGL
TLASMLNDVP ISRWDAGAGS 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
//
