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Database: UniProt
Entry: S1NTW0_9ENTE
LinkDB: S1NTW0_9ENTE
Original site: S1NTW0_9ENTE 
ID   S1NTW0_9ENTE            Unreviewed;       799 AA.
AC   S1NTW0;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=I568_00798 {ECO:0000313|EMBL:EOW84304.1};
OS   Enterococcus columbae DSM 7374 = ATCC 51263.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1121865 {ECO:0000313|EMBL:EOW84304.1, ECO:0000313|Proteomes:UP000014113};
RN   [1] {ECO:0000313|EMBL:EOW84304.1, ECO:0000313|Proteomes:UP000014113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51263 {ECO:0000313|EMBL:EOW84304.1,
RC   ECO:0000313|Proteomes:UP000014113};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Enterococcus columbae ATCC_51263 (PacBio/Illumina
RT   hybrid assembly).";
RL   Submitted (MAR-2013) 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:EOW84304.1}.
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DR   EMBL; ASWJ01000004; EOW84304.1; -; Genomic_DNA.
DR   AlphaFoldDB; S1NTW0; -.
DR   STRING; 1121865.OMW_00200; -.
DR   PATRIC; fig|1121865.3.peg.192; -.
DR   eggNOG; COG0744; Bacteria.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000014113; 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; 3.40.50.12800; -; 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   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: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:UP000014113};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        36..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          93..271
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          403..645
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          775..799
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   799 AA;  88607 MW;  AB25E1351FFB0494 CRC64;
     MSDKNTRNHA KIKPEPKKTS IDKFLFFNIS VRVIQALFLV MMAFIILLTA LGLGIGMGYF
     AFLVEDTKVP TKVELQQDLG DITQTSKLLY ADGTPIADIR SDLRRTNVPS NQISPWLKKA
     IVATEDEYFY KHHGVVPKAV LRALLSEAIG GAGGGGSTLT QQLVKQQILS SETTFKRKAN
     EILLALEVEK NFSKDEIITM YLNVSPFGRN NQGQNIAGVQ EAALGIFGKN ANDLTLPQAA
     FIAGLPQSPI IYSPYTNDGQ LKKDFTYGLK RKDIVLFSMY RNHDITKKEY EAAKNYDLTK
     DFLPPQQAEN TAHGYLYDEV MTQTIDLFIN KLATDDGLTN SQLDDPDIYN EYAQTAQEKL
     ANGGYTVQTT IDANVYQAMQ EAVSDYGYML DIQTGDPVEV GNVLMENQTG KILGFVGGRD
     YQTNQFNHAF DAKRQAGSAI KPVLVYGPAI DLGLIGSESR VSDYATTWKN GTDAGKEIVN
     ATNKGSNTFQ TVREALSWSN NIPAYNIYQD IIQQTGDSSF VYTNYLAKMN YPASNNWQYE
     SAPLGVTTVT ALTQTNGFQT LANRGVYQQG YMIESIKSAK GETIYQHTAN PVRVYSEAAA
     TIMNDLMRSV LKDQITTSYK SNLASLNAQL ANFDWVGKTG STNDWADSWL IVSTPSITIS
     SWSGYEDNRA TNSNAGKRTS LYLANLVNRI YQVKPTVFGN GETFSLADSV QKEKVAKFTG
     QKNQGTVKLN NAEITNFGEE TTSLWAKNGP VDTTFKFGIG GTDANYTDYW KKFSSTKKTE
     DKEEKDKKTE NQEQKNQEN
//
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