ID A0A1M5EDZ6_9BACE Unreviewed; 803 AA.
AC A0A1M5EDZ6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 18-JUN-2025, entry version 33.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN ORFNames=SAMN05444349_13429 {ECO:0000313|EMBL:SHF77407.1};
OS Bacteroides faecichinchillae.
OC Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
OC Bacteroidaceae; Bacteroides.
OX NCBI_TaxID=871325 {ECO:0000313|EMBL:SHF77407.1, ECO:0000313|Proteomes:UP000184436};
RN [1] {ECO:0000313|EMBL:SHF77407.1, ECO:0000313|Proteomes:UP000184436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26883 {ECO:0000313|EMBL:SHF77407.1,
RC ECO:0000313|Proteomes:UP000184436};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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=2.4.99.28;
CC Evidence={ECO:0000256|ARBA:ARBA00049902};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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; FQVD01000034; SHF77407.1; -; Genomic_DNA.
DR RefSeq; WP_025075902.1; NZ_SSTN01000007.1.
DR AlphaFoldDB; A0A1M5EDZ6; -.
DR STRING; 871325.SAMN05444349_13429; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000184436; Unassembled WGS sequence.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
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:InterPro.
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; IPR050396; Glycosyltr_51/Transpeptidase.
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 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000184436};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 69..227
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 305..581
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 712..798
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 803 AA; 90274 MW; F1EC2352ED15A577 CRC64;
MGGKLIKFLK HLSITRKVML SCITLLVIGY IFCLPRQLFH VPYSTVVTDR NEELLGARIA
SDGQWRFPPR ATTPEKIKQC LITFEDKHFY HHWGVNPLSI GRAFYQNTKN KRVVSGGSTL
TMQTIRLARN KSRTVSEKFI EVVLATRLEF RATKEEILSM YISHAPFGGN VVGLDAASWR
YFGHSAEDLS WAESAMLAVL PNAPAMIHLS KGRTTLLAKR NRLLKQLFEK KIIDSSTYEL
AISEPLPDEP HPLPQIAPHL VSRFYQERNG AYSRSTIDRG IQTQIEDMAE RWSNEFSRSD
IRNLAILIID IPTNQVIAYC GNVHFEQQKG GYQVDIIQAP RSTGSILKPF LYYAMLKEGS
LLPHTLLPDI PININGFTPQ NFSLQFEGAV PASEALARSL NIPAVTMLQK YGVPKFHHFL
QQIGFKTINK PSSHYGLSLI LGGAEATLWD VTNAYAEMGR ILLVQKDDAY NILSQNEKAH
ILLAMNGEEE TNTYELFNHQ TKNKQSPFII QKEGLKEASG AAWQTLSALT EVNRPEEIDW
KSIPSMQTIA WKTGTSYGFR DAWAVGVTPR YAVGVWVGNA TGEGKPGLVG AQTAGPVLFD
IFNLLPSSSW FASPTGIFVE AEVCKQSGHL KGRFCEETDT LLILPIGLRT EACPYHHQIT
LSTDESHRVY ENCANTEPTI QKSWFTLPPV WEWYYKQHHP EYKPLPPFKA GCGEDAIQTM
QFIYPSMNAH IKLPKQMDGS KGFMTVELAH ANANETIFWH LDNSYITQTQ NFHNISLQPS
PGKHLLTAVD SKGNTVSTTF FIE
//
