ID D9X992_STRVT Unreviewed; 502 AA.
AC D9X992;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Secreted esterase {ECO:0000313|EMBL:EFL32093.1};
GN ORFNames=SSQG_02611 {ECO:0000313|EMBL:EFL32093.1};
OS Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 /
OS Tue 494).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=591159 {ECO:0000313|EMBL:EFL32093.1, ECO:0000313|Proteomes:UP000004184};
RN [1] {ECO:0000313|Proteomes:UP000004184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494
RC {ECO:0000313|Proteomes:UP000004184};
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 "Annotation of Streptomyces viridochromogenes strain DSM 40736.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GG657757; EFL32093.1; -; Genomic_DNA.
DR AlphaFoldDB; D9X992; -.
DR STRING; 591159.SSQG_02611; -.
DR eggNOG; COG5555; Bacteria.
DR HOGENOM; CLU_016303_1_0_11; -.
DR Proteomes; UP000004184; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 4.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR23221; GLYCOSYLPHOSPHATIDYLINOSITOL PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR23221:SF7; PHOSPHATIDYLINOSITOL-GLYCAN-SPECIFIC PHOSPHOLIPASE D; 1.
DR Pfam; PF01839; FG-GAP; 4.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR PROSITE; PS51470; FG_GAP; 2.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000004184};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..502
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003131972"
SQ SEQUENCE 502 AA; 49740 MW; FDF5E5836983F698 CRC64;
MPQSTSKRRI GRGVGVAAAV AVVAAVTAPV AAHAATDAGP AEPAATKLHD DLNGDGYADL
AVAAPSATVG GKKGAGYVAV VYGSKNGLDI TTRQVLSQST AGVPGSPETD DAFGSALTTA
DLDRDGYADL VVGVGREDTA DGGAESGMAE VLWGGPQGLT GGPVLATGKA HDGLGGQGRL
TVGDVNGDGA ADLVTVANQH DLRVLNGPFT RAGGTAHGEQ VVKDEFDSRV LDLAAGDVNG
DGVTDVAASE NDGDEYDARR VVYWPGSPRG LSPYTTVKGG DGYRLQGGEN LDIGDVDQDG
VDDIVVGRAV DGYDSDLDTP LAKGGRVSLI PGTPDGPDGA HATFLNQDSP GVPGSAERGD
GFGTDVRIAD VDGDGHPDVA TGLPGEDLDG VTDAGAVVVL RGTAQGLTGT GAQVVTQNTP
DVPGAAEQGD TFGGAVHLAD ADHDGLADLA VGAPGENGKA GSVWYFRSGP STVVSPNGTT
TFGNTLLGTS ATNARLGTAF AG
//
