ID C6VXS4_DYAFD Unreviewed; 766 AA.
AC C6VXS4;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN OrderedLocusNames=Dfer_3903 {ECO:0000313|EMBL:ACT95107.1};
OS Dyadobacter fermentans (strain ATCC 700827 / DSM 18053 / CIP 107007 / KCTC
OS 52180 / NS114).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=471854 {ECO:0000313|EMBL:ACT95107.1, ECO:0000313|Proteomes:UP000002011};
RN [1] {ECO:0000313|EMBL:ACT95107.1, ECO:0000313|Proteomes:UP000002011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700827 / DSM 18053 / CIP 107007 / KCTC 52180 / NS114
RC {ECO:0000313|Proteomes:UP000002011};
RX PubMed=21304649; DOI=10.4056/sigs.19262;
RA Lang E., Lapidus A., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H.,
RA Cheng J.F., Land M., Hauser L., Chang Y.J., Jeffries C.D., Kopitz M.,
RA Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA Mavrommatis K., Chen A., Palaniappan K., Chain P., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Goker M., Rohde M., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Dyadobacter fermentans type strain (NS114).";
RL Stand. Genomic Sci. 1:133-140(2009).
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};
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DR EMBL; CP001619; ACT95107.1; -; Genomic_DNA.
DR RefSeq; WP_015813351.1; NC_013037.1.
DR AlphaFoldDB; C6VXS4; -.
DR STRING; 471854.Dfer_3903; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; dfe:Dfer_3903; -.
DR eggNOG; COG4953; Bacteria.
DR HOGENOM; CLU_006354_7_3_10; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000002011; Chromosome.
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:InterPro.
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; IPR011815; PBP_1c.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02073; PBP_1c; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR Pfam; PF06832; BiPBP_C; 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002011}.
FT DOMAIN 44..220
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 299..538
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 677..761
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 766 AA; 86367 MW; D08E51925A299977 CRC64;
MKKNRVRKAL LALICLIALF FALDLVFPFK PNIHYATQIT DREGRVIHAF LSREDKWRLY
SNVDEITPLL RKTLIYKEDQ YFYYHPGVNP FAVVRAAARN VFSGKRTSGA STITMQVVRL
MDPRPRTYLN KFIEMWHAVQ LEMHYSKAEI LQFYINLVPY GGNIEGIKAA SLLYFGKAPQ
LLSLAEITAL TIVPNRPSGL RPGTRNDALR EARNSWLKRF QEDGLFDTPV IRDALAEPLN
IRRLQTPRLA PHLSIRLKQQ FPDEPVIRTH VNMQAQSQIE EQVKNYINRR QLMNIHNAAV
LVVNNETMEV EAYVGSADFN NPFDGGQVDG VRAVRSPGST LKPLLYAAAF DAGMITPKSV
LNDVPGNFSG YEPENFDKHF NGAVTTEFAL ANSLNIPAVK VLKEIGTPAL IAKLRKARFK
TVDKQAKNLG LSMILGGCGV TLEELTRLFA AFANEGKLRN LRLSGADVQD KNGTTFLSEE
ATFLTTGILT QITRPDLPTN FDNTYHLPRI AWKTGTSYGK RDAWSIGYNR RYTVGVWVGN
FSGEGVPELS GANTATPLLF SIFNALDYNS PKGWYKTPAN ISTRNVCPVS GDIPSDFCDH
QVPDQYILGV SAYHKCQHMR WVFTDAKGKM SYCTYCLPES GFEKKAYPNL APELIAFYEM
QKLPYPKIPP HNPLCERVFH EGAPLIVSPN DGSEYYIRKD EPQQIQLACQ AANDVQEVYW
YINDKLFQKS SPQESIFLTP PLGRVKVSCS DDKGRNADVW IVVKRM
//
