ID V6J188_9BACL Unreviewed; 880 AA.
AC V6J188;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=P343_02200 {ECO:0000313|EMBL:EST13580.1};
OS Sporolactobacillus laevolacticus DSM 442.
OC Bacteria; Bacillota; Bacilli; Bacillales; Sporolactobacillaceae;
OC Sporolactobacillus.
OX NCBI_TaxID=1395513 {ECO:0000313|EMBL:EST13580.1, ECO:0000313|Proteomes:UP000018296};
RN [1] {ECO:0000313|EMBL:EST13580.1, ECO:0000313|Proteomes:UP000018296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 442 {ECO:0000313|EMBL:EST13580.1,
RC ECO:0000313|Proteomes:UP000018296};
RX PubMed=24371202;
RA Wang H., Wang L., Ju J., Yu B., Ma Y.;
RT "Genome Sequence of Sporolactobacillus laevolacticus DSM442, an Efficient
RT Polymer-Grade D-Lactate Producer from Agricultural Waste Cottonseed as a
RT Nitrogen Source.";
RL Genome Announc. 1:e01100-13(2013).
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 -!- 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:EST13580.1}.
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; AWTC01000001; EST13580.1; -; Genomic_DNA.
DR RefSeq; WP_023508752.1; NZ_AWTC01000001.1.
DR AlphaFoldDB; V6J188; -.
DR STRING; 1395513.P343_02200; -.
DR PATRIC; fig|1395513.3.peg.444; -.
DR eggNOG; COG0744; Bacteria.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000018296; 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; 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:SF11; PENICILLIN-BINDING PROTEIN 1B; 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:UP000018296};
KW Transferase {ECO:0000313|EMBL:EST13580.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 39..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 98..281
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 466..707
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 817..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..850
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 880 AA; 98232 MW; 07B4DD16142268A1 CRC64;
MHAPLKSFSD FFDRLAEKWA SSSVIRTIHS ITGVIWNSLL LTLAILVIGL FFAAGTVSGY
FAALVRDQPV LSYKTLNHDI NNYSESSVSY FAGKIPIGNM NSDLVRTKTK LKDMSPYLIH
AVVATEDELF YQHHGVVPKA VIRASMEELL NKPQVTGGSS ITQQLVKNQI LTNEVSLERK
FKEILLALRL ERFFTKDQIL ESYLNMASFG RDASGKNVAG ASTAAEGIFG VKADKLSLAQ
AAFIAGLPKN PFTYSPFQNH GGLKKDLSAG INRAHTVLKR MYAVGYINKT QLDSAMKYDY
KKHFAKPEKS INSDYPYLMK EVQNRSTVIL AKQMAQKQGY SSDKLYTDYL NYKKMVYEHN
NNIYREKSLQ EIAKIHKYDF SAVQKHYSLF NEFMKNAAID LENGGYRIYT TINKPIYDDM
TSFAQNYSGY SPDQYARNKD GQILEVKNSK TGKMEKVKDP MQVGSILIEN KTGRIISFVG
GRGFGTSELN YATEVTRQNG STMKPLLVYA PAMELDLIQP GSILPDLPYK RIVNGQVYEP
TDYGSTSSSK LFHGFETARA ALAASHNVPA VSVFTRLNNT TNSAPDYLRK MGITSLVGSD
GYNVSAALGG ITRGITIEEN TNAYTTFANN GSFVDAYMID KITDSTGKLI YQHKVQPVRV
FSEQTNYLML DMMRDVFKYG TGAALPGMLH FSADWAGKTG TSQDWRDSWL VASNPNITMG
VWNGYAHNQR LNQHTYSTQT KQLWAGFANS AYDVDPDLMA PKEHFSQPQG IEKTTYCGLT
DGKPTAYCKA AGFEETDLMN VKYLPKEAQE VLEPLNGQPQ SDQSVAQQGQ PDQNNQNQQP
NEQQPADNSL FRINPDFMKS HFPFTDLNAA NPDLLGKIRP
//
