ID A0A0C1CRT5_9FLAO Unreviewed; 770 AA.
AC A0A0C1CRT5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-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=OA85_04470 {ECO:0000313|EMBL:KIA86891.1};
OS Flavobacterium sp. AED.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1423323 {ECO:0000313|EMBL:KIA86891.1, ECO:0000313|Proteomes:UP000031403};
RN [1] {ECO:0000313|EMBL:KIA86891.1, ECO:0000313|Proteomes:UP000031403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AED {ECO:0000313|EMBL:KIA86891.1,
RC ECO:0000313|Proteomes:UP000031403};
RA Gale A.N., Newman J.D.;
RT "Flavobacterium sp. AED Genome.";
RL Submitted (OCT-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 -!- 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:KIA86891.1}.
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DR EMBL; JSYM01000001; KIA86891.1; -; Genomic_DNA.
DR RefSeq; WP_039108291.1; NZ_JSYM01000001.1.
DR AlphaFoldDB; A0A0C1CRT5; -.
DR STRING; 1423323.OA85_04470; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000031403; 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: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; 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:SF11; PENICILLIN-BINDING PROTEIN 1B; 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 27..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 74..247
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 430..684
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 770 AA; 86795 MW; A1A574C12DD7D7C3 CRC64;
MAIKKNNNQT KNIDKDITYY KKKFWKIFFY GMGIIALFFL FASWGLFGSM PSFEDLENPD
SNLATEIISA DGVVLGKYFE KNRSQLKYSD LPKNLVQALV ATEDARFYEH SGIDGRGTLR
AIASLGTSGG ASTLTQQLAK QLFHGEGSKF LPFRIVQKVK EWIIAIRLER QYTKNEIIAM
YCNVYDFGNN SVGVSSAAKT YFSKEPKDLT IDESAILVGM FKNSGLYNPV RNPQGVKNRR
NVVLLQMEKA GIITDPQKLN LQSLPITLHF KLETHKDGTA TYFREYLRDY MKKWVEENKK
PDGSDYDIYK DGLKIYTTID SRMQLHAEEA VSAHMANLQE EFFIQSKGNK NAPFVNISEV
ETQRILNQAM KSSHRWEVLK SMDKSDEEIL ASFKEKTKMK VFTWKGERDT IMTPLDSIRY
YKHFLQSGLM AMEPQTGNIK AWVGGINYKY FQYDHVGQGA RQVGSTFKPF VYATAIEQLN
MSPCDSIIDG PFMIHKGRHH VTEDWEPKNS DNRYRGMVTL KQGLANSINT VSAKLMDKVG
PEAVVDLAHK LGIKSEIPVQ PSIALGAVEI TVQDMVAAYS TFANQGVYMK PQFITRIEDK
SGVVIYEPIP ESHDVLNKDI AFAVIKLLEG VTEGGSGERL RTSGGGNGDN RWTGYPYSFR
NPIAGKTGTT QNQSDGWFMG MVPNLVTGVW VGCEDRSARF KTITYGQGAT AALPVWGYFM
KLCYDDPGLH VSKSDFDRPA NLSIKVDCYT PRAVVKDTTN IQQDTEEFEL
//
