ID L7F2V0_9ACTN Unreviewed; 545 AA.
AC L7F2V0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Hydrolase, alpha/beta domain protein {ECO:0000313|EMBL:ELP64945.1};
GN ORFNames=STRTUCAR8_08342 {ECO:0000313|EMBL:ELP64945.1};
OS Streptomyces turgidiscabies Car8.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=698760 {ECO:0000313|EMBL:ELP64945.1, ECO:0000313|Proteomes:UP000010931};
RN [1] {ECO:0000313|EMBL:ELP64945.1, ECO:0000313|Proteomes:UP000010931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Car8 {ECO:0000313|EMBL:ELP64945.1,
RC ECO:0000313|Proteomes:UP000010931};
RX PubMed=21087627; DOI=10.1016/j.plasmid.2010.11.002;
RA Huguet-Tapia J.C., Badger J.H., Loria R., Pettis G.S.;
RT "Streptomyces turgidiscabies Car8 contains a modular pathogenicity island
RT that shares virulence genes with other actinobacterial plant pathogens.";
RL Plasmid 65:118-124(2011).
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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:ELP64945.1}.
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DR EMBL; AEJB01000419; ELP64945.1; -; Genomic_DNA.
DR RefSeq; WP_006380016.1; NZ_AEJB01000419.1.
DR AlphaFoldDB; L7F2V0; -.
DR STRING; 85558.T45_02762; -.
DR PATRIC; fig|698760.3.peg.6215; -.
DR Proteomes; UP000010931; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013595; Pept_S33_TAP-like_C.
DR PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ELP64945.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010931};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..545
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039727499"
FT DOMAIN 422..521
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
FT REGION 519..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 545 AA; 58480 MW; 5ED7C4194D5D4768 CRC64;
MRAAALYSAA GSLLLTTLAA APADSAPGLP GRPGGPGSAE FRGSVLAAAR AGAAGIRFGE
CPAAEELPDS VRCGTVTVPL DYAHPDGKQI KLTVSRTEAT GKNPRDPEHK VERQGALVYN
PGGPGASGMF FPMIGVIPEW KRIAGAYDLV GYAPRGVARS APLSCKDPKH FFKGPTQAPV
HPSESYKRER VAEAKAYARG CAERSGDALR HYHSLNNARD LDVLRAALGE DRLTFMGASY
GTYFGALYAT LFPSHVRRMV FDSVVNPDPG QIWYRNNLDQ STAFESRWAD FRAWTARHDD
VYGLGATPAA VLRSYEKAAA RLAAEPAGGK VGPGQLQGAF LQAGYYDDYW PHRAHALSAY
LKGDPQPLID QAAPVTEAAV EAENGNAVYT AVECNDAPWP TSWQVWDRDN TRLARTAPFE
TWDNAWMNLP CAFWQAPRQT PLDVRTGPGD LPPVLILAAE RDAATPYAGA LELRRRLPGS
ALVTERGAGT HGIAGGPNRC VNDYLDAYLL AGRLPGRSAD CAPHAEPRPA ARVDRSQKEK
AARAS
//
