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Database: UniProt
Entry: D9XL29_9ACTN
LinkDB: D9XL29_9ACTN
Original site: D9XL29_9ACTN 
ID   D9XL29_9ACTN            Unreviewed;       507 AA.
AC   D9XL29;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Fusidic acid esterase {ECO:0000313|EMBL:EFL40225.1};
GN   ORFNames=SSRG_03029 {ECO:0000313|EMBL:EFL40225.1};
OS   Streptomyces griseoflavus Tu4000.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=467200 {ECO:0000313|EMBL:EFL40225.1, ECO:0000313|Proteomes:UP000002968};
RN   [1] {ECO:0000313|EMBL:EFL40225.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tu4000 {ECO:0000313|EMBL:EFL40225.1};
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 griseoflavus strain Tu4000.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GG657758; EFL40225.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9XL29; -.
DR   STRING; 467200.SSRG_03029; -.
DR   eggNOG; COG5555; Bacteria.
DR   HOGENOM; CLU_016303_1_0_11; -.
DR   Proteomes; UP000002968; 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   PANTHER; PTHR23221; GLYCOSYLPHOSPHATIDYLINOSITOL PHOSPHOLIPASE D; 1.
DR   PANTHER; PTHR23221:SF7; PHOSPHATIDYLINOSITOL-GLYCAN-SPECIFIC PHOSPHOLIPASE D; 1.
DR   Pfam; PF01839; FG-GAP; 3.
DR   Pfam; PF13517; FG-GAP_3; 1.
DR   PRINTS; PR01185; INTEGRINA.
DR   SMART; SM00191; Int_alpha; 6.
DR   SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR   PROSITE; PS51470; FG_GAP; 2.
PE   4: Predicted;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   507 AA;  50693 MW;  9EE0BFA48278B188 CRC64;
     MNSRTGTRGR PYPAASRTRQ ETPLHKNLRT ALATATAAAL TGGLLVAMAG PAAAAPGLDG
     DFNGDGYRDV AVTAPLANVS GKANAGAVTI LYGSPKGAGA AKIQTLSQNS AGVPGTAEKD
     DQFGAHTAPG DFNGDGYADL AVGAPGEDAG TDTNGGTVVI LWGGSGGLSG GTTVPDPTRS
     VHDWFGQVVA AGDYDGDGRA DLAIASDINK VDIYRGGFTK SGSTGGRYTV TAPILKVKGT
     DIFNLTPGDI DADGRTDLVV DGYEGDSDGD YSYNANYWLP GSSSGATTSG AQKLPAGVIS
     DIGDVDGDGY GDIVIGNSWD PGTDTPGTAK GGSVEIIYGT SYGPEGAAET VSQNTAGVPG
     SNETGDNFGY EVSLGDINGD GHDDLVIGAP GEDLGEFKDA GMVSVIYGWN GGLSETGTQS
     LHQDIPGVPG GNETGDGFGG EVLLSDVTGD GKADLTVGLP WENEANGYAV AFNSDGSKID
     TTGRGIGLTQ AGLSSAGNPM FGFHING
//
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