ID J5GPX6_9FIRM Unreviewed; 997 AA.
AC J5GPX6;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=HMPREF1140_1516 {ECO:0000313|EMBL:EJP22095.1};
OS Lachnoanaerobaculum sp. ICM7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnoanaerobaculum.
OX NCBI_TaxID=936594 {ECO:0000313|EMBL:EJP22095.1, ECO:0000313|Proteomes:UP000006599};
RN [1] {ECO:0000313|EMBL:EJP22095.1, ECO:0000313|Proteomes:UP000006599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICM7 {ECO:0000313|EMBL:EJP22095.1,
RC ECO:0000313|Proteomes:UP000006599};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) 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 -!- 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}.
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:EJP22095.1}.
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DR EMBL; ALJL01000022; EJP22095.1; -; Genomic_DNA.
DR RefSeq; WP_009663061.1; NZ_ALJL01000022.1.
DR AlphaFoldDB; J5GPX6; -.
DR PATRIC; fig|936594.3.peg.1171; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000006599; 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; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT DOMAIN 93..266
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 444..731
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 845..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 997 AA; 107166 MW; 3910C9AC7A236479 CRC64;
MNKENENKTP EKSSKSPGSR KKKYINKFIF QAVKTFFLAL LVVAVLGGAM AVGMIKGIID
NAPDVDVDSI VPLGYATTVY NASGQVTDTL VMAGSNREEV TYDELPKVLI DAFVAIEDSR
FWKHNGIDTR AILRAVSGVI TGNSSSGGGS TITQQLIKNN VFNGGRERSF GEKVERKFQE
MYLAVKLEKQ MDKKLILTNY LNTINLGSNS LGVKVAARRY FGKEVSDLTL SEATVIAGIT
KGPTKYNPIT GQEANSERRK IILQYMYEQG YITKEQQEEA LADDVYSRIQ NINTLAKEKN
NHYSYFTDAL ISQVTSAFIN ELGYTETQAH NLLYSGGLSI YTTQDPSLQQ IVDSEVNNPE
NYPDTKYALE YRLTVTDSEK NTHNYSEKDI NKYHSDVLHD GFNGLYTTED AAKADAESYK
ATVVKDGDTV VGESVKTVLE PQVSFVLMDQ KTGAVKAING GRGEKTSSLS LNRATNTTRQ
PGSTFKVISS FAPALDTSGD TLATTYYDAE YTIGEKTFQN WYDKQGYMGW SSIRDGIIYS
MNIVALKTLM ETVTPRVGVQ YAKDFGISTL TDQDYNASLA LGGLTKGVTN LELTGAFATI
ANQGVYTKPV FFTKIVDHNG KTLIDNTAPQ NHRVIKDSTA FLLTDAMAAS TENNRKFASS
GININSTSTR AHLDNMSVAG KSGTTSKNVD VWFVGFTPYY TAGVWAGCDE NQTLSDNGGT
SFHKDIWRKI MTKVSEGSED IGFPVPDSVE TAVVCRKSGK LPIPGVCDHD PRGDSTYTEY
FAKGTVPTEV CDHHTTVTVC SESGLLPTAN CPTTVTKVAL IVPSGQSNTD DSQYAVPTAT
CTIHGGPSQI IDPNAPTAND GDDAGVGVSP RAGVNHPIVN PKQNNVTVGV APNGDVVGAA
PGSNSSGQSP NTIVAPTKAN SNSSKPKRQP SEIKIPETTT ASPIKTGPSS KEPDDSDVLH
GPGVTPTTEA PRSGPGAHMS TEGPGGQGSP VLIGPGQ
//
