ID A0A1M6VUM3_9FLAO Unreviewed; 791 AA.
AC A0A1M6VUM3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SAMN05444407_101368 {ECO:0000313|EMBL:SHK85099.1};
OS Chryseobacterium contaminans.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1423959 {ECO:0000313|EMBL:SHK85099.1, ECO:0000313|Proteomes:UP000184069};
RN [1] {ECO:0000313|EMBL:SHK85099.1, ECO:0000313|Proteomes:UP000184069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27621 {ECO:0000313|EMBL:SHK85099.1,
RC ECO:0000313|Proteomes:UP000184069};
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=2.4.1.129;
CC Evidence={ECO:0000256|ARBA:ARBA00023988};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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DR EMBL; FRBM01000001; SHK85099.1; -; Genomic_DNA.
DR RefSeq; WP_066690596.1; NZ_MAYF01000001.1.
DR AlphaFoldDB; A0A1M6VUM3; -.
DR STRING; 1423959.SAMN05444407_101368; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000184069; 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 29..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 81..257
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 444..671
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..791
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 791 AA; 89226 MW; 4CE286302B5864A6 CRC64;
MEVNNKNAGN KGKTFPLPPK KKNTSWKKWV SFIWIGLIAV VLGISGLFFA VSQGFLGEMP
DVKELENPDI FVASEIISSD GVTLGKFEKE KTQPIVYKDL PPYLIYALQA KEDERFKEHS
GIDLYSIARA VAYGGGRGGG STITQQLAKL LFTGTASQNK IERAFQKLKE WVVAVSLEKR
YTKEEIITLY FNKFDFLFNA NGVEMASRVY FNKKTSELTL PEAATFVAML ENPRKNNPYR
YPEKAKERRN VVLDQMQKTG YIDAATYEKA INTPVEVDFH PIKSITDGYS AYYKFYLRKE
IDKYLESHEK ETGKKLNLYK DGLKIYVTLD SKMQKYAEEA IKEHLTDLQK RFDAEQRGRK
NRPFYYLTDK QINDVMVQAM KRTGRYKLLK ADGMPDDSIM MEFKKPIKTS RFTWAGEEEV
EMSPWDSIRY HKQIAQAGLM SMVPGTGEIK AWVGGIDWQH FQYDHIKQGK RQVGSTFKPF
VYATAIMKLG MTPCSTVSNG TYDHNGWHVP GRGGMLTLKD GLAHSQNPIA ARLIEMTGVD
AVIQTARDLG VTEDIPRNNT IALGSSDITI YEMLGAYSTF ANYGNYNKPE MIWRIEDANG
RVIKEVNVEP KEVMNPMYAY TMIELMKGVA QYGTASGELG RRGISKGVEI AAKTGTTQNN
SDGWFMGITP KLATGAWVGW EDRATHFFGT GEGQGARMAL PIWAIFMKKV WADKTLGITP
DDKFTKPSDW KDGCSNLKGL GGGYGDDGSL QTIDEIKNPR PVDPTPKKPT EKKEENINEN
LHSNDEVDFN K
//
