ID A0A1M6JRC1_9FLAO Unreviewed; 783 AA.
AC A0A1M6JRC1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 18-JUN-2025, entry version 32.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN ORFNames=SAMN04488508_109205 {ECO:0000313|EMBL:SHJ49212.1};
OS Aquimarina spongiae.
OC Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aquimarina.
OX NCBI_TaxID=570521 {ECO:0000313|EMBL:SHJ49212.1, ECO:0000313|Proteomes:UP000184432};
RN [1] {ECO:0000313|Proteomes:UP000184432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22623 {ECO:0000313|Proteomes:UP000184432};
RA Varghese N., Submissions S.;
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; FQYP01000009; SHJ49212.1; -; Genomic_DNA.
DR RefSeq; WP_073320141.1; NZ_FQYP01000009.1.
DR AlphaFoldDB; A0A1M6JRC1; -.
DR STRING; 570521.SAMN04488508_109205; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000184432; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000184432};
KW Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 60..223
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 301..561
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 690..776
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 783 AA; 88319 MW; 8884273234CD0713 CRC64;
MFQRIKTYIK NHPKRIVLIT ILLVWYYFSL PSTLFKDPTA TVVESVDGEL VGAKIAKDGQ
WRFPETDSVP TKFAKCIIAF EDQQFYNHPG FNPIAIVDAM IDNSKAGKIV RGGSTLTQQV
IRLSRKGKKR TYFEKLKELI LATRLEWGKS KSDILKLYAS HAPFGGNVVG VDMAAWRYFG
LPAHQLSWAE SATLAVLPNA PSLIYPGKNQ ERLLKKRNRL LKTLLEQQTI DSLTYTLSIQ
ETLPQRPYRL PQIAPHLVDN IAKKHKGERV QTTLRLALQK QVNDIVKKHY DQLRQNEVYN
MAVLVLDVET RNVLSYVGNT PTDKTHQKDV DIIQAPRSTG STLKPLLYAA MMDKGELLPE
QLVSDIPTVI AGYNPKNFDE TYSGAVPANR ALARSLNVPA VRLLQQYGLQ RFRDELNAFQ
IKDIQYSADH YGLSLIVGGA EANLWDLCKT YAGMAGTLNH FLESSSEYFT NEFAEPILEK
NSEVDFGKPI KEKLIFGAGS IWLTFEAMKE VNRPEGDDAW EFYDSSKEIA WKTGTSYGNR
DAWAIGATSK YVVGVWIGNA DGEGRPEVTG LTAAAPVLFD VFNIVPDTKW FATPYDDLVT
TTVCAQSGHI AGEHCPKKTI NVSLSGTKTE PCTYHRLIHL DKERRYQVNS SCESVDNMIH
ESWFVLPSLQ AYYFKNNNAD YHELPSFLPG CSTVDEDRMD FIFPKANSSV YLPKGFDGKT
NEVVLKIAHT NPEAQVFWYV DEQFVGATRQ FHEMPILPEP GKHLITILDE NGNELKRVLE
VKE
//
