ID A0A0C2V4B3_9BACL Unreviewed; 984 AA.
AC A0A0C2V4B3;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=KP78_36960 {ECO:0000313|EMBL:KIL43872.1};
OS Jeotgalibacillus soli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Jeotgalibacillus.
OX NCBI_TaxID=889306 {ECO:0000313|EMBL:KIL43872.1, ECO:0000313|Proteomes:UP000031938};
RN [1] {ECO:0000313|EMBL:KIL43872.1, ECO:0000313|Proteomes:UP000031938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P9 {ECO:0000313|EMBL:KIL43872.1,
RC ECO:0000313|Proteomes:UP000031938};
RA Goh K.M., Chan K.-G., Yaakop A.S., Ee R., Gan H.M., Chan C.S.;
RT "Genome sequencing of Jeotgalibacillus soli.";
RL Submitted (JAN-2015) 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:KIL43872.1}.
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; JXRP01000020; KIL43872.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2V4B3; -.
DR STRING; 889306.KP78_36960; -.
DR PATRIC; fig|889306.3.peg.3712; -.
DR Proteomes; UP000031938; 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:UP000031938};
KW Transferase {ECO:0000313|EMBL:KIL43872.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 98..283
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 422..663
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 900..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..975
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 984 AA; 107944 MW; 7653AAD2F4CFDE02 CRC64;
MNERIKDLRK RATSFFTRFN SGSWRKNTRI SYQVFWNICL ILIILGVMGG AFAGGVGAGY
FASLVKDEEI IPFEMMESNI YDYTETSDLY FANDVYLGKL RTDLEREEVV LENVSPYLIN
AVIATEDEYF MEHDGVVPKA IMRALFQEVT NSAVQTGGST LTQQLIKNQI LTNEVSFDRK
AKEILLALRL ERFFEKDEII EAYLNVADMG RNSSGRNIAG VQTAAKGIFG VEAKDLTLPQ
AAFIAGLPQA PFGYTPFTNV GERKDEAGLQ PGLQRMQEVL SRMLREESIT QEEYDQALAY
DITADFIPAS SSSIDEYPWV TRELESRATE IIAVVLAERD GYSEQQLEDS KPLKDEYEQL
ADRDIRQNGY KIHSTIDKEL YDAMEEVKNN FNDFGPNHNV TRTNLETEEE VIVSEPVQVG
GILLENGTGR IISFTGGRDF DQEQLNHATQ SYRSSGSTIK PIAVYAPAIE FGLIGAGTPL
ADVKFSYRGW NPDNYSYREY GLVPARTALA ASHNLSAARL YGKMQSQGLN PGEFLEKMNP
EKISSAEYEN PSFSLGGMAT GISVEENTAA YATLGNMGQY VEPYMIEKIV DKNGEVIYEH
KTESIQVYSP ATAYITLDMM RDTMTPIGTG RSAPRFLNFT TDWAAKSGTS QDFHDNWFIA
TNPNITFGMW FGYGEPESLY DNGQYNTRTI NLWANMMNRA NELRPELIDP PNSFQQPDGV
VNRAFCSFTG QAATDACSQA GLVTSDLFPS SFAFSGASDA LLVSRYVTLN GVRYVALDST
PAEFSSNGAL LSPDYAEQML APYGGNAAGL FPEGNSFFDN LLVAQNRLED DGSNPAGVTA
TATGSGITWT PSGSGDVVGY RVKNTGGSTI VSRKADENLT ASLPNGTYYV VAVDVAGKES
TPSNEIQIGA PTLPPPAQEK EENDAPATPV PPTTPPPSSG NGGNEEDPPE ETEPPEVTEP
AEEEQPAEET PPEETPPPDE GNGE
//
