ID A0A428N7C6_9BACI Unreviewed; 966 AA.
AC A0A428N7C6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, 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=D7Z54_06790 {ECO:0000313|EMBL:RSL34258.1};
OS Salibacterium salarium.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX NCBI_TaxID=284579 {ECO:0000313|EMBL:RSL34258.1, ECO:0000313|Proteomes:UP000275076};
RN [1] {ECO:0000313|EMBL:RSL34258.1, ECO:0000313|Proteomes:UP000275076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IM0101 {ECO:0000313|EMBL:RSL34258.1,
RC ECO:0000313|Proteomes:UP000275076};
RA Yamprayoonswat W., Boonvisut S., Jumpathong W., Sittihan S., Ruangsuj P.,
RA Wanthongcharoen S., Thongpramul N., Pimmason S., Yu B., Yasawong M.;
RT "Draft genome sequence of Bacillus salarius IM0101, isolated from a
RT hypersaline soil in Inner Mongolia, China.";
RL Submitted (OCT-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 -!- 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:RSL34258.1}.
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DR EMBL; RBVX01000004; RSL34258.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428N7C6; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000275076; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1310.40; -; 1.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR013783; Ig-like_fold.
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:SF32; PENICILLIN-BINDING PROTEIN 2A; 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 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000275076};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 30..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 90..270
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 404..663
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 791..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..918
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 966 AA; 106765 MW; 917AEEEC772AF7AF CRC64;
MRNFFEKLNN NIDNMKDKPV IKSLNITSQV FWNLLLILFV SLIMLTLFAG GAGAGYFLSL
IDDQKAYSQE EFQNTIFDYE ETSGIYFSEG EFLGEIPAEL ERKERSLDDM SDNLVNAVIS
TEDEYFFEHD GIVPKALLRA TYQEVTNAET QTGGSTLTQQ VVKNQILTNE VSFDRKAKEI
ALAMRMEQYF DKEEILEAYL NIVPFGRNSD GQNIAGAQSA SEGIFGVDAS ELNPAQAAFI
AGLPKNPYTY TPFAQGGEVK ESFEAGLNRM ELVLGNMREN DFITEEEYQK ALEYNIRENL
TGPTESSLDD YPYLTNETQR RAKEIILDDL LEESDINLED LDEEERQEYD MQAGNELAVG
GYNVHITIQK DIYDAMQNAI ASSQWFGPDK VEKDGEGTVQ EEVGAMMIDN NSGAILSFVG
GRDFNVQNLN HATQTRRQNG STMKPLLAYG PAMEKGLVQP GTVLPDVPGE FSNGEGYTNY
GGGYEGFVSV RKGLKESRNS PAVRTFEKIV NLDHDIARNA LLDLGFTNVA PAEPYPSAAI
GAFGTTVEQN TNAFSTFGNN GEYNDSYMIE KIETKDGEVI FEQSPESNEV FSPQTTFLMV
DMLRDVLDPG GTAGALPGMM NFGGDWAGKT GTTNDTRDSW FVGFNPNVTF GTWIGYDDPQ
TIENYHGLSY GARTQQIWSD MMNAAYEADE ETLGLEDQFE QPNGIVRQTI CGISGKLPST
RCQEAGLTTT DYFNEKYLPS QSDDSLESEP FVTINGNRYL AYDSTPSEFT QTGVSIDEDL
FDVEEVGEYL PDDWDNITPD TKAPNNGRTP SPVANVSYNN GELTWSAHSD NDIVGYRIYS
DNGSSIGSVQ GDNTSFSIGS GSYFVTAIDS VGRESNQSAT TEGSNQNDND DEEENEEDSD
SSDDNTDNNE DNNSEDDSSS NEDNNNNNSD DNSENNTENE PNDNSEDQND SGNGNSNDDE
NEDSAD
//
