ID A0A1I7FDY3_9BRAD Unreviewed; 740 AA.
AC A0A1I7FDY3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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=SAMN05192541_101402 {ECO:0000313|EMBL:SFU34378.1};
OS Bradyrhizobium arachidis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=858423 {ECO:0000313|EMBL:SFU34378.1, ECO:0000313|Proteomes:UP000199591};
RN [1] {ECO:0000313|EMBL:SFU34378.1, ECO:0000313|Proteomes:UP000199591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 26795 {ECO:0000313|EMBL:SFU34378.1,
RC ECO:0000313|Proteomes:UP000199591};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FPBQ01000001; SFU34378.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7FDY3; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000199591; 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 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 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 86..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 142..308
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 394..625
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 28..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 740 AA; 79301 MW; 35EFBC6215009193 CRC64;
MAWGKKKGGR KEPLFGLPAA LADLRLTAAD RIPGGDDTPK KSTKSSAKRK ADEPDEEPPR
ERKAQPSRSG AKRRSKSRGG FGLGRLIYWG AVLSLWGVIA VIGVVIYVGA HLPPIQSLEI
PKRPPTIQIV GIDGSMLAQR GEMAGANVAL KDLPPYLPKA FIAIEDRRFY SHFGIDPIGI
LRALVTNVLH RGVSQGGSTL TQQLAKNLFL TQERTMQRKL QEAELAIWLE RKHSKNEILE
LYLNRVYFGS GAYGVEAAAQ KYFGKSAKNV TVAEAAMLAG LVKSPSRLAP NRNPEGAEAR
AQIVLAAMAD AKFITDAQAQ ASIGHPSYNV KPAGAGTVNY VADWIGEVLD DLVGQIDESI
KVETTIDPKL QSVAEAAIID ELAAKSVKFN VSQGALVAMT PDGAVRAMVG GRNYSESQYN
RAVTAKRQPG SSFKPFVYLT ALEQGLTPDT VRQDAPIEVK GWKPENYTHE YFGAVTLTQA
LAMSLNTVAI RLGLEVGPKN VVRTAHRLGI SSKLEPNASI ALGTSEVSVV ELVGAYAPFA
NGGFAVTPHV VTRIRTLSGK LLYMRQPDER NQVIDPRYVG MMNAMMRETL ISGTAKKAEI
PGWPAAGKTG TSQDYRDAWF IGYTASLVTG VWLGNDDNSP TKKATGGGLP VEVWSRFMKT
AHEGVPVAAL PNSQASWGLS NLAQAASQIS PPTPAAPGLA PAPVSNGGYR PPPPTRANVR
PEAAAGLDGW LMDRLFGGNR
//
