ID J7Q8E8_METSZ Unreviewed; 745 AA.
AC J7Q8E8;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN OrderedLocusNames=BN69_1471 {ECO:0000313|EMBL:CCJ06922.1};
OS Methylocystis sp. (strain SC2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylocystaceae; Methylocystis.
OX NCBI_TaxID=187303 {ECO:0000313|EMBL:CCJ06922.1, ECO:0000313|Proteomes:UP000005263};
RN [1] {ECO:0000313|EMBL:CCJ06922.1, ECO:0000313|Proteomes:UP000005263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:CCJ06922.1,
RC ECO:0000313|Proteomes:UP000005263};
RX PubMed=23045511; DOI=10.1128/JB.01446-12;
RA Dam B., Dam S., Kube M., Reinhardt R., Liesack W.;
RT "Complete Genome Sequence of Methylocystis sp. Strain SC2, an Aerobic
RT Methanotroph with High-Affinity Methane Oxidation Potential.";
RL J. Bacteriol. 194:6008-6009(2012).
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; HE956757; CCJ06922.1; -; Genomic_DNA.
DR RefSeq; WP_014890953.1; NC_018485.1.
DR AlphaFoldDB; J7Q8E8; -.
DR STRING; 187303.BN69_1471; -.
DR KEGG; msc:BN69_1471; -.
DR PATRIC; fig|187303.17.peg.1603; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_7_5; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000005263; Chromosome.
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; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 117..282
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 373..614
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 711..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 745 AA; 80604 MW; 3BBDCA96B46757B7 CRC64;
MLERFQASAF AKRLRRILLA VDALIDSAMF QSGRRARELY EDFSTFMERF HVSGLARVGV
ELSCEALTLG LGAGIVAMAL ASSAFQMTSD ENWLKQTDLA VTFLDRYGAE VGQRGIKHDD
AVPLEQYPDH LIKAVLATED RRFYEHFGID VIGTLRALTV NARSSGVVQG GSSISQQLAK
NLFLSNERTI TRKINEAFLA LWLEHHLTKR EILKLYLDRV YMGGGAFGIQ AAAEFYFGKS
VKDVTLAEAA MLAGLFKAPT KYAPHVNLPA ARARANDVLN NLVDAGFMTD SQIIAAQRSP
ATPIDRARET SPDWYLDYAY GEIRKLAQDG KLGDNRVLSV RTTLDSNVQK RAEDVIETNL
REQGRSFHVK QSAAVVMEPD GAVRAIVGGR DYGASQFNRA TDAARQPGSS FKPYVYLTAL
MTGRFKPTTI VTDRPTCIGN YCVHNYSGGY AGSMPLAMAL AKSLNTVAIQ LSQAIGKGDS
RIGRAKIIET CRRLGITTPL EDTPSLPVGQ SDVIPLEHSA AYGAFVNGGK KVTPYAAVEI
RNRQGDLLYR HDRDAPPQTQ AVPLDKVVEL AGMMKKVVEE GTGKRAQLGE GIDVIGKTGT
TNGYKDAWFC GYSGTMGGCV WYGNDDNAPM NNMTGGTLPA GTWHDIMAYA HQGAILKPIV
GLRPDPKGAT AAVNANVVKP LELGAPQRPA TLSRGAMQAL ESLQMKIKAV GGDKQSGLEA
PDPAASDVDR REAQRASGAA VGVIR
//
