FBPC3_RHOJR
ID FBPC3_RHOJR Reviewed; 346 AA.
AC Q0RYP7;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Fe(3+) ions import ATP-binding protein FbpC 3 {ECO:0000255|HAMAP-Rule:MF_01706};
DE EC=7.2.2.7 {ECO:0000255|HAMAP-Rule:MF_01706};
GN Name=fbpC3 {ECO:0000255|HAMAP-Rule:MF_01706};
GN OrderedLocusNames=RHA1_ro08545;
OS Rhodococcus jostii (strain RHA1).
OG Plasmid pRHL1.
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=101510;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1;
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC -!- FUNCTION: Part of the ABC transporter complex FbpABC involved in Fe(3+)
CC ions import. Responsible for energy coupling to the transport system.
CC {ECO:0000255|HAMAP-Rule:MF_01706}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Fe(3+)(out) + H2O = ADP + Fe(3+)(in) + H(+) + phosphate;
CC Xref=Rhea:RHEA:12332, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.7; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01706};
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (FbpC),
CC two transmembrane proteins (FbpB) and a solute-binding protein (FbpA).
CC {ECO:0000255|HAMAP-Rule:MF_01706}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01706};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01706}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Fe(3+) ion
CC importer (TC 3.A.1.10) family. {ECO:0000255|HAMAP-Rule:MF_01706}.
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DR EMBL; CP000432; ABG99589.1; -; Genomic_DNA.
DR RefSeq; WP_007297804.1; NC_008269.1.
DR AlphaFoldDB; Q0RYP7; -.
DR SMR; Q0RYP7; -.
DR EnsemblBacteria; ABG99589; ABG99589; RHA1_ro08545.
DR KEGG; rha:RHA1_ro08545; -.
DR HOGENOM; CLU_000604_1_1_11; -.
DR OMA; INMLPLK; -.
DR Proteomes; UP000008710; Plasmid pRHL1.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0015408; F:ABC-type ferric iron transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR CDD; cd03259; ABC_Carb_Solutes_like; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR015853; ABC_transpr_FbpC.
DR InterPro; IPR030287; FbpC.
DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013611; Transp-assoc_OB_typ2.
DR PANTHER; PTHR24220:SF675; PTHR24220:SF675; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF08402; TOBE_2; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50331; SSF50331; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51242; FBPC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Ion transport; Iron; Iron transport; Membrane;
KW Nucleotide-binding; Plasmid; Reference proteome; Translocase; Transport.
FT CHAIN 1..346
FT /note="Fe(3+) ions import ATP-binding protein FbpC 3"
FT /id="PRO_0000272047"
FT DOMAIN 5..235
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01706"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01706"
SQ SEQUENCE 346 AA; 35950 MW; F57F6AA8E2172BDC CRC64;
MTYALEVDGV DKSFGGATIL RGVAFAVEPG STTAIVGPSG CGKTTLLRLI AGFEKPDAGT
IALAGRVVAG GGWTPAHRRS VGYVAQDGAL FPHATVGANV GFGLPRRART PARIAELLEM
VSLDPSFAVR RPDQLSGGQQ QRVALARALA REPELMLLDE PFSALDAGLR ANTRRIVADV
LAKAAITTIL VTHDQPEALS FAGRVAVMSA GRLAQIGTPR EIYSTPIDVA TAEFIGDAVV
LSAHVDGGRA HCALGDVAVA SNGVHGNARV MLRPEQIEVT TDGAGMSGTV VDVEYLGSEM
LLGIRLDTGD GEVPERVTVR RFGATALTPG DRVGIRVLGQ AVAYDI