ID Q9FBN9_STRCO Unreviewed; 716 AA.
AC Q9FBN9;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN OrderedLocusNames=SCO5039 {ECO:0000313|EMBL:CAC05884.1};
GN ORFNames=SCK7.12 {ECO:0000313|EMBL:CAC05884.1};
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226 {ECO:0000313|EMBL:CAC05884.1, ECO:0000313|Proteomes:UP000001973};
RN [1] {ECO:0000313|EMBL:CAC05884.1, ECO:0000313|Proteomes:UP000001973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145
RC {ECO:0000313|Proteomes:UP000001973};
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.H.,
RA Kieser T., Larke L., Murphy L., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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; AL939122; CAC05884.1; -; Genomic_DNA.
DR RefSeq; NP_629191.1; NC_003888.3.
DR AlphaFoldDB; Q9FBN9; -.
DR STRING; 100226.gene:17762688; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR PaxDb; 100226-SCO5039; -.
DR PATRIC; fig|100226.15.peg.5117; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_6_0_11; -.
DR InParanoid; Q9FBN9; -.
DR OrthoDB; 8865355at2; -.
DR PhylomeDB; Q9FBN9; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IBA:GO_Central.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IBA:GO_Central.
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:SF34; PENICILLIN-BINDING PROTEIN 1A; 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:UP000001973}.
FT DOMAIN 32..209
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 320..567
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 628..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..694
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 716 AA; 76860 MW; 0B91C806C290E221 CRC64;
MGAFIVLYMM IDIPEGNPEA DLQSNVYKYS DGSIMARTGE RNREIVDLAK IPKDVQRTFV
AAENKTFYND AGVDLKGTAR GVLNTLSGKG AQGGSTITQQ YVKNYYLTQE QTVSRKLKEL
VISLKLDREK SKDYILAGYI NTSYYGRGAY GIQAAAQAYY RVDAEDLTVE QGAYLSALLQ
APNQYDWAIA SETGKKLVQQ RWNYVLDNMV EQKWLGAGDR QGMKFPEPKE PKAAAGKEGQ
VGYLVDAADH ALKKQLVAQG AAEDMEQAKA LVDLGGYTVT LNIDKKKQAA LEAAVKKQLT
SKLDPDERKV DADVQAGAAS VDPKTGSVVA MYGGVNYLKH FTNNATRDDY QPASTFKPVI
LAAAVDHDAE TQDGVPITAN TLYDGDSERP VMDGDKKVGF APPNEDDHDY GEIDVQEAMN
KSVNSVFAQM GIDVGMPEVM KVAADLGMDT EGEQAVPAQT LGSMGASPLE MAGVYATFDN
HGKKVTPAIV KSVEHKDRKV EMPDPIGEQV ISREAADTVT SVLTGVVNDG TAKKSVRENP
LRDGQKVAGK TGTSDNNKSA WFSGFTPGLV TSVGLFGEDD EPPHKQVPMY KAAGVDYRVN
GGGPPAEIWA AYTFGVMDEV TEFDLETKQG AAVRPSKSPT APESPTKSPT REETSEAPPP
SSDPTTEAPP SSDPTTEEPP ESPTNSPSNS PSTEPPPDGG STESGDPELP GVDWGQ
//
