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Database: UniProt
Entry: A0A166SQY3_9RHOB
LinkDB: A0A166SQY3_9RHOB
Original site: A0A166SQY3_9RHOB 
ID   A0A166SQY3_9RHOB        Unreviewed;       570 AA.
AC   A0A166SQY3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE   Flags: Fragment;
GN   ORFNames=A3721_17020 {ECO:0000313|EMBL:KZY04113.1};
OS   Sulfitobacter sp. HI0023.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Sulfitobacter.
OX   NCBI_TaxID=1822225 {ECO:0000313|EMBL:KZY04113.1, ECO:0000313|Proteomes:UP000077323};
RN   [1] {ECO:0000313|EMBL:KZY04113.1, ECO:0000313|Proteomes:UP000077323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI0023 {ECO:0000313|EMBL:KZY04113.1,
RC   ECO:0000313|Proteomes:UP000077323};
RA   Sosa O.A.;
RT   "Microbial cycling of marine high molecular weight dissolved organic
RT   matter.";
RL   Submitted (MAR-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}.
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:KZY04113.1}.
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DR   EMBL; LWEQ01000107; KZY04113.1; -; Genomic_DNA.
DR   RefSeq; WP_068101158.1; NZ_LWEQ01000107.1.
DR   AlphaFoldDB; A0A166SQY3; -.
DR   OrthoDB; 9766909at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000077323; Unassembled WGS sequence.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077323};
KW   Transferase {ECO:0000313|EMBL:KZY04113.1}.
FT   DOMAIN          9..191
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          279..516
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KZY04113.1"
FT   NON_TER         570
FT                   /evidence="ECO:0000313|EMBL:KZY04113.1"
SQ   SEQUENCE   570 AA;  60745 MW;  A205EFC754637A98 CRC64;
     WRGDQFGGVV TADSVSPHLR NAVIATEDRR FYRHFGVSPR GIASAIRINL SEGRGPLQGH
     GGSTITQQTA KLLCLGEPYE PSSGQTEKEY EAECRRNSLQ RKAKEALFSM AMEAKYSKDD
     ILSIYLNRAY MGGGAFGAEA ASQRFFGKPA AAVTPAEGAM LAGLLTAPTT LSPTNNLDRS
     QERAATVIRL MRQQGYLSEA EAQDAIANPA QLSEAAEAEA GGYFADWVMS SGPEFFTRNT
     TEDVIIKTTL DQRIQKAAED GLRAIFENKV REGSKAQAAI VVMSADGAVR ALVGGRKTKV
     AGAFNRATQA MRQTGSAFKP FVYAAALDLG YSPNDLVEDA PYCLNIPGSG EWCPKNYTNN
     FKGAVTLTEA LKESLNIPAV KISENVGREI VSQVASQFGI KSDLAAGPAL ALGASESTLL
     EMTGAYAGIL NGGSSVTPYG LIDLRLLGDS EPLMGTGGGI GERVIQEEAA RQLVYMMEKV
     ISEGTGQRGQ FGGRELAGKT GTTSAAKDAW FIGFSADYVT GVWMGYDDNT PLEGVTGGGL
     PTDIWREVML RVHEGLPMNP LPMMTPLPST
//
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