FPUA_BACAN
ID FPUA_BACAN Reviewed; 324 AA.
AC Q81L65; E9QR41; E9QR42; Q6HSL7; Q6KLW1;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Petrobactin-binding protein FpuA {ECO:0000305};
DE AltName: Full=Petrobactin receptor {ECO:0000303|PubMed:22429808};
DE Flags: Precursor;
GN Name=fpuA {ECO:0000303|PubMed:20487286};
GN OrderedLocusNames=GBAA_4766 {ECO:0000312|EMBL:AAT33889.1};
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 IN PETROBACTIN UPTAKE, AND DISRUPTION PHENOTYPE.
RX PubMed=20487286; DOI=10.1111/j.1365-2958.2009.07025.x;
RA Carlson P.E. Jr., Dixon S.D., Janes B.K., Carr K.A., Nusca T.D.,
RA Anderson E.C., Keene S.E., Sherman D.H., Hanna P.C.;
RT "Genetic analysis of petrobactin transport in Bacillus anthracis.";
RL Mol. Microbiol. 75:900-909(2010).
RN [3]
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).
RN [4] {ECO:0007744|PDB:6ALL}
RP X-RAY CRYSTALLOGRAPHY (2.47 ANGSTROMS).
RA Stogios P.J.;
RT "Crystal structure of a predicted ferric/iron (III) hydroxymate siderophore
RT substrate binding protein from Bacillus anthracis.";
RL Submitted (AUG-2017) to the PDB data bank.
CC -!- FUNCTION: Part of an ABC transporter complex involved in ferric-
CC petrobactin uptake. {ECO:0000269|PubMed:20487286,
CC ECO:0000269|PubMed:22429808}.
CC -!- SUBUNIT: Can probably form at least three ABC transporter complexes,
CC composed of two ATP-binding proteins (FpuC or FpuD), two transmembrane
CC proteins (FpuB) and a solute-binding protein (FpuA), or composed of two
CC ATP-binding proteins (FatE), two transmembrane proteins (FatC and FatD)
CC and a solute-binding protein (FpuA). {ECO:0000305|PubMed:22429808}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303};
CC Extracellular side {ECO:0000305|PubMed:22429808}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant exhibits a growth defect in iron-
CC depleted media. Mutant is able to produce and secrete petrobactin, but
CC petrobactin accumulates in the culture supernatants. Mutant is also
CC significantly attenuated in a murine model of inhalational anthrax.
CC {ECO:0000269|PubMed:20487286}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 8 family.
CC {ECO:0000305}.
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DR EMBL; AE017334; AAT33889.1; -; Genomic_DNA.
DR RefSeq; WP_000722819.1; NZ_WXXJ01000026.1.
DR PDB; 6ALL; X-ray; 2.47 A; A/B=1-324.
DR PDBsum; 6ALL; -.
DR AlphaFoldDB; Q81L65; -.
DR SMR; Q81L65; -.
DR STRING; 260799.BAS4424; -.
DR DNASU; 1083866; -.
DR EnsemblBacteria; AAT33889; AAT33889; GBAA_4766.
DR GeneID; 45024400; -.
DR KEGG; bar:GBAA_4766; -.
DR PATRIC; fig|1392.230.peg.4697; -.
DR HOGENOM; CLU_038034_10_1_9; -.
DR OMA; GIWMFGG; -.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR InterPro; IPR002491; ABC_transptr_periplasmic_BD.
DR Pfam; PF01497; Peripla_BP_2; 1.
DR PROSITE; PS50983; FE_B12_PBP; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Ion transport; Iron; Iron transport;
KW Lipoprotein; Membrane; Palmitate; Reference proteome; Signal; Transport.
FT SIGNAL 1..17
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 18..324
FT /note="Petrobactin-binding protein FpuA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_5011757700"
FT DOMAIN 54..324
FT /note="Fe/B12 periplasmic-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00344"
FT LIPID 18
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 18
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:6ALL"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:6ALL"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:6ALL"
FT HELIX 60..67
FT /evidence="ECO:0007829|PDB:6ALL"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:6ALL"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:6ALL"
FT HELIX 80..85
FT /evidence="ECO:0007829|PDB:6ALL"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6ALL"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:6ALL"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:6ALL"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:6ALL"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:6ALL"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:6ALL"
FT HELIX 129..133
FT /evidence="ECO:0007829|PDB:6ALL"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:6ALL"
FT TURN 143..147
FT /evidence="ECO:0007829|PDB:6ALL"
FT HELIX 150..165
FT /evidence="ECO:0007829|PDB:6ALL"
FT HELIX 168..191
FT /evidence="ECO:0007829|PDB:6ALL"
FT STRAND 198..207
FT /evidence="ECO:0007829|PDB:6ALL"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:6ALL"
FT HELIX 221..227
FT /evidence="ECO:0007829|PDB:6ALL"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:6ALL"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:6ALL"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:6ALL"
FT HELIX 250..256
FT /evidence="ECO:0007829|PDB:6ALL"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:6ALL"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:6ALL"
FT TURN 273..278
FT /evidence="ECO:0007829|PDB:6ALL"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:6ALL"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:6ALL"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:6ALL"
FT HELIX 306..321
FT /evidence="ECO:0007829|PDB:6ALL"
SQ SEQUENCE 324 AA; 36074 MW; 0EAD6197AE43B3A6 CRC64;
MKKILSIFIV VFLFAVGCGQ QKEEKKETKA DNKNQAITIK HAEGETKLDK PAKKVVVLEW
VYSEDLLALG VQPVGMADIK NYNKWVNTKT KPSKDVVDVG TRQQPNLEEI SRLKPDLIIT
ASFRGKAIKN ELEQIAPTVM FDPSTSNNDH FAEMTETFKQ IAKAVGKEEE GKKVLADMDK
AFADAKAKIE KADLKDKNIA MAQAFTAKNV PTFRILTDNS LALQVTKKLG LTNTFEAGKS
EPDGFKQTTV ESLQSVQDSN FIYIVADEDN IFDTQLKGNP AWEELKFKKE NKMYKLKGDT
WIFGGPESAT SLATQVADVM TAKK
