ID A0A369QB43_9SPHN Unreviewed; 758 AA.
AC A0A369QB43;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=HME9302_01653 {ECO:0000313|EMBL:RDC60446.1};
OS Alteripontixanthobacter maritimus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Alteripontixanthobacter.
OX NCBI_TaxID=2161824 {ECO:0000313|EMBL:RDC60446.1, ECO:0000313|Proteomes:UP000253727};
RN [1] {ECO:0000313|EMBL:RDC60446.1, ECO:0000313|Proteomes:UP000253727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HME9302 {ECO:0000313|EMBL:RDC60446.1,
RC ECO:0000313|Proteomes:UP000253727};
RA Kang H., Kim H., Joh K.;
RT "Altererythrobacter sp. HME9302 genome sequencing and assembly.";
RL Submitted (APR-2018) 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 -!- 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}.
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:RDC60446.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QBKA01000002; RDC60446.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369QB43; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000253727; 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: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 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 Glycosyltransferase {ECO:0000313|EMBL:RDC60446.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:RDC60446.1};
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:UP000253727};
KW Transferase {ECO:0000313|EMBL:RDC60446.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 101..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 144..314
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 395..631
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 659..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..678
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 758 AA; 82757 MW; 634ACAE1D6080192 CRC64;
MKGNSPITRW WRSRLRDSDT GPSAWDSSGY FGDTADGMAD RAAAGYDRPA QPDEAWRSDY
SYDPAYEYQQ DPYAPASYRT GWRRFVPVLG KRSRWWWLRK GLVAGFVLFL ALVAWLAFTA
PLSKSLEPLV PPQITLLAAD GTPIARKGSV VDQPVQAAAL PDHVIEPFLA IEDRRFYSHW
GIDPRGLGRA VWANVSGGRV EGGSTITQQL AKFTFLTPER SMTRKAREML IAFWLETWLT
KDEILERYLS NAYFGDNVYG LRAASLHYFY RQPEKLKPAQ AAMLAGLVQA PSRLNPVKHY
ARAEKRMRLV IGSMVAAGYI TQGEADAMAA PRLDVRTESN LPTGTYFADW ALPQARKLAG
GGYARQTMST TLDARLQSFA RKAVGRAKLG EAQVALVAMR TNGEIVAMVG GKDYKASAFN
RVTQAKRQPG STFKLFVYLA ALREGWEPED TIDNSEIVKG SYRPKNARGR YSPTITLEDG
LAQSSNVAAV RLLREVGDEA VIETARDLGV TAPLAKGDPS LALGTSNMTL LELTAAYAGV
AANRFPVEPT AFPAEEPGWL DWLTDGKDSI SGSDQASMER MLRSAINRGT GRAAMLPGPN
YGKTGTTQDN RDALFVGYAG ELVVGVWIGN DDNSSLGAIS GGTTPARIWR DFMRQAQGLG
APKAPAPAPR PSDPGGPVEP MDVPDLDDIP DGDIPLGNGD ARMRVEDDAV TVSTEIDGLP
IELRVDQDGF RVSPAPGQPP TPRPPPDRRE PADPRDRR
//
