ID D4J3Z3_9FIRM Unreviewed; 875 AA.
AC D4J3Z3;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
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=CC1_00870 {ECO:0000313|EMBL:CBK79064.1};
OS Coprococcus catus GD/7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Coprococcus.
OX NCBI_TaxID=717962 {ECO:0000313|EMBL:CBK79064.1, ECO:0000313|Proteomes:UP000008798};
RN [1] {ECO:0000313|EMBL:CBK79064.1, ECO:0000313|Proteomes:UP000008798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GD/7 {ECO:0000313|EMBL:CBK79064.1,
RC ECO:0000313|Proteomes:UP000008798};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Coprococcus catus GD/7.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBK79064.1, ECO:0000313|Proteomes:UP000008798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GD/7 {ECO:0000313|EMBL:CBK79064.1,
RC ECO:0000313|Proteomes:UP000008798};
RA Pajon A.;
RL Submitted (MAR-2010) 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 membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane
CC protein {ECO:0000256|ARBA:ARBA00004606}.
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DR EMBL; FP929038; CBK79064.1; -; Genomic_DNA.
DR AlphaFoldDB; D4J3Z3; -.
DR STRING; 717962.CC1_00870; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; cct:CC1_00870; -.
DR PATRIC; fig|717962.3.peg.420; -.
DR HOGENOM; CLU_006354_2_2_9; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008798; 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; 1.
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; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF11; PENICILLIN-BINDING PROTEIN 1B; 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 4: Predicted;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycosyltransferase {ECO:0000313|EMBL:CBK79064.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CBK79064.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000313|EMBL:CBK79064.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT DOMAIN 88..265
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 440..686
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 782..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 875 AA; 95449 MW; 7931856CC1AE371C CRC64;
MDYSKQNNEK KRKKIRSNAA KSKKKITFNI FRFTMLAILL IVIVGIAAAI GGFKGVIDSA
PDITASNVMP SKLKSVMYYP DGQEAIELVG AQSNRTIVSI DDIPKCLSNA FVAIEDNRFY
EHNGIDPKGI VRALFVGLSH GGNFSEGAST ITQQLIKLTI FNGGAETDTI QRFKRKFQEW
YLALKLEKEM SKDEIMEAYL NTINLGRGAY GVEAAAERYF NKKCSDLTVS ESAVIAAIAQ
SPSYNNPIDY PDINAQRRDK ILNNMLTLGL ITQQQYDEAK ADDVYSRITE VNKTTKSKDI
IYTWFEDAAI DQVLNDLQEK LGYTSAEANN ALYSGGLQIY LTQSRHIQDI VDSYYNDDDN
FPSTEYRLHW ALTYKDKDGE TVNIDENSLQ SYYGADDCDL LYDNEDQAKQ SISEFLEAKG
ITDDDIIAQS FDMTVQVQSS FVLMDQSTGY VLALSGGRGE KKTSRSFNRA TQSTRQPGSV
FKTIAVFLPA LDSCGLSLAS TKEDEPYTTP DGYQPFNTNA NSYQGTTTIR EAITYSMNVV
TTKWLVEDVT PKLGIEYLEN LGITTMDEDR DAYAPLGLGG ISNGVTNLEL TGAYAAIANG
GVYTEPILYS KILDKDGNVL LDNVPEKHTA MKDSTAWLLT SAMEDVVSKG TGTSAQISNY
GIAEAGKTGT TDDYKDLWFV GYTPYYTAGI WFGYDDSTLM RYRLGRNYNA HKVLWKNIMN
EVLEGYEDRD FVMPSDVEKI RVCSSTGLLA SYGCNVITEY FAKDTAPTEY CSKHSYRYYE
NSYDDDSSSS SSSGSNSSNT TSGDNSGNAN SGADNSGGNN SGGDNSGGGN SGGDNSGGDN
SGSDNSGGDN SGGGNSGSDN SGGDNSGGDN TGAEQ
//
