ID B5GDM5_STRSH Unreviewed; 779 AA.
AC B5GDM5;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE Flags: Fragment;
GN ORFNames=SSBG_02026 {ECO:0000313|EMBL:EDY44421.3};
OS Streptomyces sp. (strain SPB074).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=465543 {ECO:0000313|EMBL:EDY44421.3, ECO:0000313|Proteomes:UP000002779};
RN [1] {ECO:0000313|Proteomes:UP000002779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPB074 {ECO:0000313|Proteomes:UP000002779};
RG The Broad Institute Genome Sequencing Platform;
RA Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Straight P., Clardy J.,
RA Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., Lander E.,
RA Galagan J., Nusbaum C., Birren B.;
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDY44421.3, ECO:0000313|Proteomes:UP000002779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPB074 {ECO:0000313|Proteomes:UP000002779};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Streptomyces sp. strain SPB74.";
RL Submitted (OCT-2009) 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};
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DR EMBL; GG770539; EDY44421.3; -; Genomic_DNA.
DR AlphaFoldDB; B5GDM5; -.
DR OrthoDB; 8865355at2; -.
DR Proteomes; UP000002779; Unassembled WGS sequence.
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: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: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}.
FT DOMAIN 87..255
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 354..614
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 779
FT /evidence="ECO:0000313|EMBL:EDY44421.3"
SQ SEQUENCE 779 AA; 81784 MW; 8FD1DBA6C5C30B8D CRC64;
MAAGDGEGEG EPPKKKGRKS RKRKGWRRLF PTWRMTLGGL VLLILLLGGA LAVGYATTDI
PAGNQEAQLQ SNVYYYDDGT LLARDGTVNR VNVKLSEIPK SVQRTVLAAE DRDFYSESAV
DPAAMVRAAW NTATGKGKQS GSTITQQYVK NYYLDQDQTV TRKAKEFFIS LKLDREKSKD
EILEGYLNTS YFGRNAYGIQ AAARAYYDKD VGQLTIPEGA YLASLLNAPS AYDVVVYPEN
RRAAEARWSY VLDGMVKQHW MTKAQRAQAK FPVPKEPTST NSSLSGQRGY LVEAVKNYLG
ENGIDKNHLT NQGYRITTTF KKSNQDALVK AVNDRLIDKL DKKNRPADRN VRAGAVSIDP
KTGRVLAMYG GIDWVKQYTN NATRADFQVG STFKPFVFTS ALENHSTTQG GETIMPATMY
DGTSKRPVKG SSIPFSPENE DQRDYGRIPV SVATDKSVNS VYAQMAVDVG PAKVKKTAEA
LGLAKGTPSL APYPSIALGT ATPSVLRMTE AYATLANHGE HNPAQLVVKI TDRDGKRVEL
PGRKSTRAVK REAADTTTSI LQSVVEKGTA MAARTSGRPA AGKTGTAEED TAALFAGYTP
DLATVVSVMG QDPETAKHVP LYGALGVARM NGGGPPTEIW AQYVKQALKG KKAHDFDLKL
AKGAKRKPPV SQAPSDSNSP GTGTGTGRSD PPASPPASGD DGNGSGEQNG TGDTTGGTPS
GGPVTPPGGG TPSGGATEPG GGDNGGTGPG GTDPGGDAGG AGGAGGAGGA GGAGFGGAG
//
