YFIY_BACSU
ID YFIY_BACSU Reviewed; 325 AA.
AC O31567; Q79EW3;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Probable siderophore-binding lipoprotein YfiY;
DE Flags: Precursor;
GN Name=yfiY; OrderedLocusNames=BSU08440;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8946165; DOI=10.1093/dnares/3.4.257;
RA Yamamoto H., Uchiyama S., Sekiguchi J.;
RT "Cloning and sequencing of a 27.8-kb nucleotide sequence of the 79 degrees-
RT 81 degrees region of the Bacillus subtilis genome containing the sspE
RT locus.";
RL DNA Res. 3:257-262(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP INDUCTION.
RC STRAIN=168;
RX PubMed=12354229; DOI=10.1046/j.1365-2958.2002.03113.x;
RA Baichoo N., Wang T., Ye R., Helmann J.D.;
RT "Global analysis of the Bacillus subtilis Fur regulon and the iron
RT starvation stimulon.";
RL Mol. Microbiol. 45:1613-1629(2002).
RN [4]
RP SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=14730579; DOI=10.1002/elps.200305676;
RA Bunai K., Ariga M., Inoue T., Nozaki M., Ogane S., Kakeshita H., Nemoto T.,
RA Nakanishi H., Yamane K.;
RT "Profiling and comprehensive expression analysis of ABC transporter solute-
RT binding proteins of Bacillus subtilis membrane based on a proteomic
RT approach.";
RL Electrophoresis 25:141-155(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, POSSIBLE SUBUNIT, DISRUPTION PHENOTYPE, AND
RP INDUCTION.
RC STRAIN=168;
RX PubMed=16672620; DOI=10.1128/jb.188.10.3664-3673.2006;
RA Ollinger J., Song K.-B., Antelmann H., Hecker M., Helmann J.D.;
RT "Role of the Fur regulon in iron transport in Bacillus subtilis.";
RL J. Bacteriol. 188:3664-3673(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290 AND THR-302, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
RN [7]
RP INTERACTION WITH FLOT, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=23651456; DOI=10.1111/mmi.12252;
RA Bach J.N., Bramkamp M.;
RT "Flotillins functionally organize the bacterial membrane.";
RL Mol. Microbiol. 88:1205-1217(2013).
CC -!- FUNCTION: Part of the ABC transporter complex YfiYZ/YfhA/YusV involved
CC in import of the iron-hydroxamate siderophores schizokinen,
CC arthrobactin and corprogen. Binds the siderophores and delivers them to
CC the surface of YfiZ/YfhA (Probable). {ECO:0000305|PubMed:16672620}.
CC -!- SUBUNIT: The complex is composed of one ATP-binding protein (YusV), two
CC transmembrane proteins (YfiZ and YfhA) and a solute-binding protein
CC (YfiY). Interacts with FloT (PubMed:23651456).
CC {ECO:0000269|PubMed:23651456, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23651456,
CC ECO:0000305}; Lipid-anchor {ECO:0000305}. Cytoplasm. Membrane raft
CC {ECO:0000269|PubMed:23651456}; Lipid-anchor. Note=Present in detergent-
CC resistant membrane (DRM) fractions that may be equivalent to eukaryotic
CC membrane rafts; these rafts include proteins involved in signaling,
CC molecule trafficking and protein secretion.
CC {ECO:0000269|PubMed:23651456}.
CC -!- INDUCTION: Induced by iron starvation, repressed by fur.
CC {ECO:0000269|PubMed:12354229, ECO:0000269|PubMed:16672620}.
CC -!- DISRUPTION PHENOTYPE: Strains lacking this gene show a reduction in
CC growth stimulation by the iron-hydroxamate siderophores schizokinen and
CC arthrobactin compared to wild-type. {ECO:0000269|PubMed:16672620}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 8 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D85082; BAA24465.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12673.1; -; Genomic_DNA.
DR PIR; C69805; C69805.
DR RefSeq; NP_388725.1; NC_000964.3.
DR RefSeq; WP_003242746.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; O31567; -.
DR SMR; O31567; -.
DR STRING; 224308.BSU08440; -.
DR iPTMnet; O31567; -.
DR jPOST; O31567; -.
DR PaxDb; O31567; -.
DR PRIDE; O31567; -.
DR DNASU; 939206; -.
DR EnsemblBacteria; CAB12673; CAB12673; BSU_08440.
DR GeneID; 939206; -.
DR KEGG; bsu:BSU08440; -.
DR PATRIC; fig|224308.179.peg.911; -.
DR eggNOG; COG0614; Bacteria.
DR InParanoid; O31567; -.
DR OMA; KHAMGTS; -.
DR PhylomeDB; O31567; -.
DR BioCyc; BSUB:BSU08440-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
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 Cell membrane; Cytoplasm; Ion transport; Iron; Iron transport; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Reference proteome; Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 21..325
FT /note="Probable siderophore-binding lipoprotein YfiY"
FT /id="PRO_0000363828"
FT DOMAIN 56..325
FT /note="Fe/B12 periplasmic-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00344"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17218307"
FT MOD_RES 302
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17218307"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 325 AA; 36304 MW; E0D8EEEA412B93D0 CRC64;
MKKHISMLFV FLMAVMVLSA CNSSESSSNS EVSSSKTRTV KHAMGTSDNI PANPKRIVVL
TNEGTEALLA LGIKPVGAVK SWKGDPWYDY LKDDMKGVKN VGLETEPNVE AIAELKPDLI
IGNKVRQEKI YDQLNAIAPT VFAESLAGNW KDNLTLYANA VNKADKGKEV IADFDKRVSD
LKNKLGDQTN KTVSVVRFLS GESRIYYTDS FPGIILDQLG FKRPEKQVEL FKKQKDQFTF
STDSKESIPD MDADVLFYFT YKADNAKENE KWANQWTSSS LWKNLKAVKS GNAHEVDDVV
WTTAGGIKAA NYLLDDIETY FLKTK
