ID J0LI39_9BACT Unreviewed; 782 AA.
AC J0LI39;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=O71_17661 {ECO:0000313|EMBL:EJF09003.1};
OS Pontibacter sp. BAB1700.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=1144253 {ECO:0000313|EMBL:EJF09003.1, ECO:0000313|Proteomes:UP000003746};
RN [1] {ECO:0000313|EMBL:EJF09003.1, ECO:0000313|Proteomes:UP000003746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB1700 {ECO:0000313|EMBL:EJF09003.1,
RC ECO:0000313|Proteomes:UP000003746};
RX PubMed=23105068; DOI=10.1128/JB.01550-12;
RA Joshi M.N., Sharma A.C., Pandya R.V., Patel R.P., Saiyed Z.M., Saxena A.K.,
RA Bagatharia S.B.;
RT "Draft Genome Sequence of Pontibacter sp. nov. BAB1700, a Halotolerant,
RT Industrially Important Bacterium.";
RL J. Bacteriol. 194:6329-6330(2012).
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 -!- 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:EJF09003.1}.
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DR EMBL; AKIS01000131; EJF09003.1; -; Genomic_DNA.
DR RefSeq; WP_007658499.1; NZ_AKIS01000131.1.
DR AlphaFoldDB; J0LI39; -.
DR PATRIC; fig|1144253.3.peg.3491; -.
DR Proteomes; UP000003746; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; 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; IPR011815; PBP_1c.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02073; PBP_1c; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR Pfam; PF06832; BiPBP_C; 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 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 60..232
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 315..554
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 697..774
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 782 AA; 88991 MW; FB9C045D671CA08C CRC64;
MSTQNITYTL PRRLLTYSKP WLRYTLHLVL LLCLTFALLN HLYPLKVNIS YSPVITASDG
SVINAFLSRD DKWRMQLEPD EINPVLKKAV LLKEDRYFYY HPGVNPFAIS RAFANNLLQN
KKTSGASTIT MQVARLLYPQ KRTYANKLYE MFRALQLEWY YSKDEILQLY LDLVPFGGNI
EGVKAASVLY FQQSPRQLSL AQAVTLTVIP NKPSSLRIGE QNERIVEFRN KWLRFYQEQG
AFPAPEIEDA LLEPLEARRQ QAPKVAPHFA YRMFRRYKNH PIVKTTLNRQ VQEKVEQLAY
NYMQRLRYQN IHNAAVLVIN NQTRAVEAYL GSADFNDFAH HGQVDGVRAV RSPGSTLKPF
LYAAAFDKGL LTPKTMITDV PVDYAGYRPQ NYFGNYNGNV TIAHALATSL NVPAVKVLDQ
LGVYTFVQKL KQAEFSEMKR KGNQLGLSLI LGGCDVKLEE LTLLYSAFAN QGRYSHIRWL
QEDTTEQETQ LLSPGAAYMT NQILTQLTRP DLPHNAHNSP NLPKIAWKTG TSYGRKDAWS
IGYNKKYTVG VWVGNFSGEG VPELNGTDSA TPLLFDIFNS IDYNSTAGWF QQPKGIGLRA
VCAESGSPAN SFCRNQVLDT FIPGISSTRK CSHLKRIAVS EDKKHSYCTS CQPATGFVQQ
LYPNHAPELL TFFDAERIPY TPIPAHNPSC SRIFKEYAPI ITSPAAGMEY FMEQEERQQL
MLHSNAHNEV KQVYWYINDK FLKATAANEK VFFEPKKAGR YKISCTDDQG RNTDSYITVK
FL
//
