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FitC

 B2L230_9PSED            Unreviewed;       719 AA.
B2L230;
10-JUN-2008, integrated into UniProtKB/TrEMBL.
10-JUN-2008, sequence version 1.
25-OCT-2017, entry version 45.
SubName: Full=FitC {ECO:0000313|EMBL:ABY91229.1};
Name=fitC {ECO:0000313|EMBL:ABY91229.1};
Pseudomonas protegens.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=380021 {ECO:0000313|EMBL:ABY91229.1};
[1] {ECO:0000313|EMBL:ABY91229.1}
NUCLEOTIDE SEQUENCE.
STRAIN=CHA0 {ECO:0000313|EMBL:ABY91229.1};
PubMed=18484997; DOI=10.1111/j.1462-2920.2008.01662.x;
Pechy-Tarr M., Bruck D.J., Maurhofer M., Fischer E., Vogne C.,
Henkels M.D., Donahue K.M., Grunder J., Loper J.E., Keel C.;
"Molecular analysis of a novel gene cluster encoding an insect toxin
in plant-associated strains of Pseudomonas fluorescens.";
Environ. Microbiol. 10:2368-2386(2008).
[2] {ECO:0000313|EMBL:ABY91229.1}
NUCLEOTIDE SEQUENCE.
STRAIN=CHA0 {ECO:0000313|EMBL:ABY91229.1};
Keel C.J.;
Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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EMBL; EU400157; ABY91229.1; -; Genomic_DNA.
RefSeq; WP_015635597.1; NZ_LHUV01000005.1.
ProteinModelPortal; B2L230; -.
GeneID; 29825860; -.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0030256; C:type I protein secretion system complex; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro.
GO; GO:0008233; F:peptidase activity; IEA:InterPro.
GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
GO; GO:0030253; P:protein secretion by the type I secretion system; IEA:InterPro.
Gene3D; 1.20.1560.10; -; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011527; ABC1_TM_dom.
InterPro; IPR036640; ABC1_TM_sf.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR010132; ATPase_T1SS_HlyB.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005074; Peptidase_C39.
Pfam; PF00664; ABC_membrane; 1.
Pfam; PF00005; ABC_tran; 1.
Pfam; PF03412; Peptidase_C39; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF90123; SSF90123; 1.
TIGRFAMs; TIGR01846; type_I_sec_HlyB; 1.
PROSITE; PS50929; ABC_TM1F; 1.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PROSITE; PS50990; PEPTIDASE_C39; 1.
4: Predicted;
ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00434};
Membrane {ECO:0000256|SAM:Phobius};
Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00434};
Transmembrane {ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAM:Phobius}.
TRANSMEM 168 190 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 202 222 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 275 298 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 304 326 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 10 131 Peptidase C39.
{ECO:0000259|PROSITE:PS50990}.
DOMAIN 168 447 ABC transmembrane type-1.
{ECO:0000259|PROSITE:PS50929}.
DOMAIN 480 715 ABC transporter.
{ECO:0000259|PROSITE:PS50893}.
NP_BIND 514 521 ATP. {ECO:0000256|PROSITE-
ProRule:PRU00434}.
SEQUENCE 719 AA; 78943 MW; FD757327143A983E CRC64;
MTRAFDAASE PSPTMLDTGL HALAWAARRF DLSISVAQLT HRLGRVEGPA DSLDLRRCAG
WIGLRARAVQ SRVQRLHHLP LPALLDTTRG WAVLDAVEGD RVRVFWPLQG QCQTLSRQEL
ATLWQGHDQG QGEVLLLAER HVQLKAGGFG VSWFLPSILK HGRQFRSVLL VSLMLQGVAL
VTPLLFENII DRVLVSRGLS SLQVLGIAML ALALFEPLFG LLRSWLFSNV ASKINAELSA
RLYQHLIQLP LGYFQRRQSG EIIARVGEMQ QIRQFLTGSA LTLVLDLAFC GLFIAVMYSY
APLLTWVVVG SLALYFLFWL CVGPLLRSRA LREYELNAAN TAFLTETVTG IETIKTGAIE
SAFQQQWQRQ LAAYVRAAFH TRIVGIWAGQ GIGLIQKLTA ALLLWWGVML VLDGQLSPGQ
LVAFNMLAGH VVEPILRLAQ VWQDFQHTLI SLRRLGDILD SDCESGSGGL ASVPALQGGV
SFQGVRFRYE EDGQEVLRQL DLEIQPGEFV GITGPSGSGK STLTRLLQRL YVPQHGRVLV
DGIDLAIADP VALRRNMSVV LQESVLFAGS VAENIRLCRP QASDAEVRHA AGLAGAAPFI
EALAQGYETE VGERGGQLSG GQRQRIALAR ALLTNPGILL LDEATSALDY ESEAAVMANL
QGIVRGRTVI SVAHRLNTLR HADRILVIDQ GRVLEQGTHQ QLLALDGLYA RQWALQMKD


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