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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//