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Database: UniProt
Entry: Q81LM1
LinkDB: Q81LM1
Original site: Q81LM1 
ID   FPUC_BACAN              Reviewed;         272 AA.
AC   Q81LM1; E9QQN5; E9QQN6; Q6HT27; Q6KMB6;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 161.
DE   RecName: Full=Petrobactin import ATP-binding protein FpuC {ECO:0000305};
DE            EC=7.2.2.- {ECO:0000305|PubMed:22429808};
GN   Name=fpuC {ECO:0000303|PubMed:22429808};
GN   OrderedLocusNames=GBAA_4595 {ECO:0000312|EMBL:AAT33716.1};
OS   Bacillus anthracis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1392;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames ancestor;
RX   PubMed=18952800; DOI=10.1128/jb.01347-08;
RA   Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA   Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT   "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL   J. Bacteriol. 191:445-446(2009).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=Sterne;
RX   PubMed=22429808; DOI=10.1111/j.1365-2958.2012.08028.x;
RA   Dixon S.D., Janes B.K., Bourgis A., Carlson P.E. Jr., Hanna P.C.;
RT   "Multiple ABC transporters are involved in the acquisition of petrobactin
RT   in Bacillus anthracis.";
RL   Mol. Microbiol. 84:370-382(2012).
CC   -!- FUNCTION: Part of an ABC transporter complex involved in ferric-
CC       petrobactin uptake. Probably responsible for energy coupling to the
CC       transport system. {ECO:0000269|PubMed:22429808}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a Fe(III)-siderophore(out) + ATP + H2O = a Fe(III)-
CC         siderophore(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:15597,
CC         Rhea:RHEA-COMP:11342, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29034, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000305|PubMed:22429808};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (FpuC),
CC       two transmembrane proteins (FpuB) and a solute-binding protein (FpuA).
CC       {ECO:0000305|PubMed:22429808}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:22429808};
CC       Peripheral membrane protein {ECO:0000305|PubMed:22429808}; Cytoplasmic
CC       side {ECO:0000305|PubMed:22429808}.
CC   -!- DISRUPTION PHENOTYPE: A mutant lacking fatE, fpuC and fpuD ATPases is
CC       deficient in petrobactin import in iron-depleted conditions.
CC       {ECO:0000269|PubMed:22429808}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; AE017334; AAT33716.1; -; Genomic_DNA.
DR   RefSeq; WP_000626544.1; NZ_VLYO01000001.1.
DR   AlphaFoldDB; Q81LM1; -.
DR   SMR; Q81LM1; -.
DR   STRING; 261594.GBAA_4595; -.
DR   DNASU; 1088621; -.
DR   GeneID; 45024240; -.
DR   KEGG; bar:GBAA_4595; -.
DR   PATRIC; fig|1392.230.peg.4533; -.
DR   HOGENOM; CLU_000604_1_11_9; -.
DR   OMA; RCWIAMA; -.
DR   OrthoDB; 9787851at2; -.
DR   Proteomes; UP000000594; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0006826; P:iron ion transport; IEA:UniProtKB-KW.
DR   CDD; cd03214; ABC_Iron-Siderophores_B12_Hemin; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR42771:SF11; FERRICHROME TRANSPORT ATP-BINDING PROTEIN FHUC; 1.
DR   PANTHER; PTHR42771; IRON(3+)-HYDROXAMATE IMPORT ATP-BINDING PROTEIN FHUC; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Ion transport; Iron; Iron transport; Membrane;
KW   Nucleotide-binding; Reference proteome; Translocase; Transport.
FT   CHAIN           1..272
FT                   /note="Petrobactin import ATP-binding protein FpuC"
FT                   /id="PRO_0000443818"
FT   DOMAIN          2..238
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         34..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   272 AA;  30996 MW;  8E221D413E734893 CRC64;
     MISVNKVFYA HSERFQMQNM NVHIKAGEVV SLIGPNGSGK STLLRLMARL LKQSEGDIVL
     DGKSIHTMKS ADVAKQLAML PQMHDHQLDL TVKELIEFGR GPHKSWRGRL NKEDEEIVDW
     ALSVTNLEGY EYRLLQSLSG GERQRAWIAM TLAQRTNVLL LDEPTTFLDI VHQLEVMELV
     KRLNEEFGMT IIMVLHDINQ AAQYSDRLLV LKRGKLQYDG VPEEVLCHEM FQHIFGIEVD
     IFQGSEKPFF TPKRISKKGG AKCEQKNVLP LS
//
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