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Database: UniProt
Entry: A0A1Q5NDN9_9ACTN
LinkDB: A0A1Q5NDN9_9ACTN
Original site: A0A1Q5NDN9_9ACTN 
ID   A0A1Q5NDN9_9ACTN        Unreviewed;       780 AA.
AC   A0A1Q5NDN9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=AMK09_04230 {ECO:0000313|EMBL:OKK24560.1};
OS   Streptomyces sp. CB02488.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703920 {ECO:0000313|EMBL:OKK24560.1, ECO:0000313|Proteomes:UP000186200};
RN   [1] {ECO:0000313|EMBL:OKK24560.1, ECO:0000313|Proteomes:UP000186200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB02488 {ECO:0000313|EMBL:OKK24560.1,
RC   ECO:0000313|Proteomes:UP000186200};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKK24560.1}.
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DR   EMBL; LIVO01000002; OKK24560.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q5NDN9; -.
DR   STRING; 1703920.AMK09_04230; -.
DR   Proteomes; UP000186200; 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; 2.
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:UP000186200}.
FT   DOMAIN          40..217
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          326..400
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   DOMAIN          413..602
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          654..780
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        666..699
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        704..724
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        734..751
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        760..780
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   780 AA;  83291 MW;  185023EBA4143C06 CRC64;
     MGVASLAYAM VTMPEVNKAA KAENNVYYWS DNTQMVATGG TANRQVIAYE QIPEAMRNAV
     ISAENKSFEH DKGIDPMGIG RAVWNMAKGG QTQGGSTITQ QYVKNSRLSQ EQTLSRKVEE
     LFITLKVGEQ GNKKEVMAGY LNVSYYGRGA SGIQAAARTY YGKDAAKLNP SECAFLATLL
     KGASYYDPAG APDVDAKEAT PAKNLDRAKK RWRWILDEEF KDGRLSKADH DKYRTFPAPK
     PLKKDAQLGG QTGYLVELAR KYFLANNTRG VTAEMLNRGG YEIHTTFDRK KVEQLNKAVK
     KVYDEKIDPK KRPDKDTHVQ FGGGSVDPET GAIKAIYGGK DATQHYTNNA DPTGAAVGST
     FKPFVLAAAM EHGRRDPELG PDQNDSQRQK VSPLSVYNGN NKLKIKKYNG EVWTNEKGEE
     WLQTNDGNHS EGNITLRKAM EVSANSPYVQ LGMDVGTDKV KEAAMAAGLK DDDNMANSTV
     PSFSIGTSSP SVIRMAGAYA TFAASGQQRE PFSVTQVKKL GEVIYQHETV TKRAFDNVVA
     DNVTDVLKNV VEHGTGTPAK LPGRDVAGKT GTTDDNLSAW FVGYTPQLST AISMYRLDDN
     EKHKGRKFEK MYGTGGEEKI HGASFPAQIW HDYMAEAMQG KKVVDFPKAE PIGDKLYGGG
     ASSPKPTPSY TPPPSPSITP SDTPPPSAPA SPPSPPDPTE SCGAWDWNCQ NNNGGTSDGG
     DNSGADAGTT GGDDGGTPGT TEGTTAGNGD PGGSSPPAGD GGNGNGNGNG NNGILGGANG
//
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