ID A0A0C5VHM1_9GAMM Unreviewed; 763 AA.
AC A0A0C5VHM1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=YC6258_00788 {ECO:0000313|EMBL:AJQ92838.1};
OS Gynuella sunshinyii YC6258.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Saccharospirillaceae; Gynuella.
OX NCBI_TaxID=1445510 {ECO:0000313|EMBL:AJQ92838.1, ECO:0000313|Proteomes:UP000032266};
RN [1] {ECO:0000313|EMBL:AJQ92838.1, ECO:0000313|Proteomes:UP000032266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC6258 {ECO:0000313|EMBL:AJQ92838.1,
RC ECO:0000313|Proteomes:UP000032266};
RA Khan H., Chung E.J., Chung Y.R.;
RT "Full genme sequencing of cellulolytic bacterium Gynuella sunshinyii
RT YC6258T gen. nov., sp. nov.";
RL Submitted (JAN-2014) 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=2.4.1.129;
CC Evidence={ECO:0000256|ARBA:ARBA00023988};
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; CP007142; AJQ92838.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C5VHM1; -.
DR STRING; 1445510.YC6258_00788; -.
DR KEGG; gsn:YC6258_00788; -.
DR PATRIC; fig|1445510.3.peg.772; -.
DR HOGENOM; CLU_006354_7_3_6; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000032266; Chromosome.
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:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:AJQ92838.1};
KW Glycosyltransferase {ECO:0000313|EMBL:AJQ92838.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AJQ92838.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000032266};
KW Transferase {ECO:0000313|EMBL:AJQ92838.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 51..227
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 303..511
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 680..758
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 763 AA; 85913 MW; E85613284B795CB6 CRC64;
MKWLLYRRFK KWIWLLACWT AMTAVIITLD TLYPVDLQSR SLSQAVLAED GTILRTFADD
NGVWRYPITL DQVSPNYLEA LLTYEDQYFY SHPGINPAAL VRAIWLWLRN GHIVSGGSTL
TMQVARIRYP EPRTVSAKLK EIIRALQLEW HYSKDDILTY YLNHAPFGGT IEGIQAAAFS
YLGHSAEHLT DAQAALLAVL PQAPSFYRPD RHPERARQAR DKLMHRLVVL GQWSPAQFED
AAIEDVQVSN LPRYQTAPLL ARRLANQYQD QNIQTFIQAQ WQQQVEELLR GYVRGIGQQV
SAAALVVDND SGKVRVYAGS ADFEDDKRFA YVDMVQAIRS PGSTLKPFIY GMALDQGLIH
SASLLMDVPL RFGDYQPDNF NGGFSGPVSV TTALQKSLNI PAVQVMERLK PVYFFLQMKQ
AGIELQLPGN ARPNLAVALG GVGTRLEDLV YAYTSLGNKG NARSLRFSTA DSASQQPLLS
EGAAWIIRKI LFDNEANVAG LAVKTGTSYG FRDAWAIAVS QHYTLGVWIG RPDGTPMPGH
YGQVTAVPLL NLIFQRLNDQ RPVPAMPDSV TETDICWPQG EWVTQDCEQL KRAYVLENTI
PTTWYSTLAR QRAFVGSDFL YWQAKDSGLR VTPDCQIPAL QQTVTVWPAP LEHWLSPELQ
RDSRIPVWDP RCHSPGTLLQ QSVLQIRGVD DQDAFQVRQN QNIQMDLYAQ GGDAPFYWFL
NGSLLPETGR RIQLKDLSSG IYQLTLMDQT GETDRIEFNV LVR
//
