FPUB_BACAN
ID FPUB_BACAN Reviewed; 678 AA.
AC Q81L64; E9R5F3; E9R5F4; Q6HSL6; Q6KLW0;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Petrobactin import system permease protein FpuB {ECO:0000305};
GN Name=fpuB {ECO:0000303|PubMed:22429808};
GN OrderedLocusNames=GBAA_4767 {ECO:0000312|EMBL:AAT33890.1};
OS Bacillus anthracis.
OC Bacteria; Firmicutes; 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, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION 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 the translocation of the
CC substrate across the membrane. {ECO:0000269|PubMed:22429808}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (FpuC or
CC FpuD), two transmembrane proteins (FpuB) and a solute-binding protein
CC (FpuA). {ECO:0000305|PubMed:22429808}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:22429808};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: A mutant lacking both fpuB and fatCD permeases is
CC incapable of using petrobactin as an iron source and exhibits
CC attenuated virulence in a murine model of inhalational anthrax
CC infection. {ECO:0000269|PubMed:22429808}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. FecCD subfamily. {ECO:0000305}.
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DR EMBL; AE017334; AAT33890.1; -; Genomic_DNA.
DR RefSeq; WP_001061683.1; NZ_WXXJ01000026.1.
DR AlphaFoldDB; Q81L64; -.
DR SMR; Q81L64; -.
DR STRING; 260799.BAS4425; -.
DR DNASU; 1083867; -.
DR EnsemblBacteria; AAT33890; AAT33890; GBAA_4767.
DR GeneID; 45024401; -.
DR KEGG; bar:GBAA_4767; -.
DR PATRIC; fig|1392.230.peg.4698; -.
DR HOGENOM; CLU_013016_7_2_9; -.
DR OMA; MFPYQIP; -.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3470.10; -; 2.
DR InterPro; IPR037294; ABC_BtuC-like.
DR InterPro; IPR000522; ABC_transptr_permease_BtuC.
DR PANTHER; PTHR30472; PTHR30472; 2.
DR Pfam; PF01032; FecCD; 2.
DR SUPFAM; SSF81345; SSF81345; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Ion transport; Iron; Iron transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..678
FT /note="Petrobactin import system permease protein FpuB"
FT /id="PRO_0000443816"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 517..534
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 584..604
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 623..643
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 650..670
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 678 AA; 72025 MW; 35EE5FCD66F7F219 CRC64;
MNNLQHTLRA SLVFGGGGAL LLLLFFIHIG QGQANISYSM IIDALISPNQ SLEHQTLIML
RLPRAVIAIL AGGALAASGV ILQTLTKNPL AESSTMGIHS GAYFFLVAAT IFLPKGLQIN
SLLFTFIGGA ITALFVYRIS GEKKGTPLRM ALAGMVVTLM LSAFTGTMQL FYENETAGLF
LWGAGSLIQN NWDGVQFSFP FIIISFLVLL GISRKLNILL LGDDVAVSLG EKTAVTRLIA
FIAAIFLTAV IVTVVGPIGF VGLVAPHLMR LIGYRQHFTL LLSSFLWGAV LLLGADVAGR
LIDPTGAELP VGAVTAMIGS PWLIYLVYRM MKSKQYMNDN GANTAGASSR YYSYKKVIII
SITLCIVTIA LGVTIGSNAY IESITNVISG QLTQFDKNMM MNLRLPRMLV AAIAGACLAI
SGLVFQGILR NPLADPSIIG ISSGAGVGAL TIMYVFPTLP GFFLPIGAFI GGLLAVGIVL
FFSWKSGFSP TALALIGIGI SALGSAIIQI FIVKANLNVA AALTWLSGST YARGWNHLEN
IILYPSLILV LIIFFLIKQL DVLVLGDDLA TGLGQPVNKT RLALIVLATL LASVNIAAVG
TIAFLGLVAP HLARIVVGMN HQRLFVCSAL FGAILLSIAD LLGRTIAYPK EIPSGLVVAV
LGAPYFLWLM RKSGKKVN
