ID A0A1G1G0L2_9BACT Unreviewed; 379 AA.
AC A0A1G1G0L2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=A2010_11135 {ECO:0000313|EMBL:OGW37573.1};
OS Nitrospirae bacterium GWD2_57_9.
OC Bacteria; Nitrospirota.
OX NCBI_TaxID=1801701 {ECO:0000313|EMBL:OGW37573.1, ECO:0000313|Proteomes:UP000176220};
RN [1] {ECO:0000313|EMBL:OGW37573.1, ECO:0000313|Proteomes:UP000176220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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 -!- 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:OGW37573.1}.
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DR EMBL; MHED01000167; OGW37573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1G0L2; -.
DR Proteomes; UP000176220; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
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 PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF00912; Transgly; 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:ARBA00022670};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 52..226
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
SQ SEQUENCE 379 AA; 42273 MW; 23FF7F102004A0F8 CRC64;
MKKILFAALA VGALGAFILA GWVVLVLSDL PDVSPLRNYR PAAAAEVLDR NGNILTQYFD
RKFRIWVPIS SLPDRVIHAV VTAEDDTFFG HNGVNYKAAW DALVHDVQKR RFARGGSTIT
QQMIKNVLLS REKTLTRKVR EYVLARRAEE ILTKRQILQI YLNEVEWGDG IYGIEAASRF
YLGKHAPDLS SAEAALLAGM LPNPRYYNPY KRPEKAKKRQ EQVLFNLFQA KRIGAEEYEA
GLRAPLGLRQ ESGASLVPAL STSSANQCCR AALERILLRL FENQNIYRGG WTVRTTLDRD
LQEELRTLEV AATGGLPDLV TVVSQEGQIR AISCSFGKES SVREKADGVL SGQEYEVVAL
PLDGITRDQI VLEADGEKK
//
