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YHFQ_BACSU
ID   YHFQ_BACSU              Reviewed;         323 AA.
AC   C0SP94; O07616; Q796T6;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Putative ABC transporter substrate-binding lipoprotein YhfQ;
DE   Flags: Precursor;
GN   Name=yhfQ; OrderedLocusNames=BSU10330;
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;
RA   Noback M.A., Terpstra P., Holsappel S., Venema G., Bron S.;
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
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   IDENTIFICATION BY MASS SPECTROMETRY, AND 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   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   -!- SUBUNIT: Interacts with FloT. {ECO:0000269|PubMed:23651456}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303, ECO:0000269|PubMed:14730579,
CC       ECO:0000269|PubMed:23651456}; Lipid-anchor {ECO:0000255|PROSITE-
CC       ProRule:PRU00303, ECO:0000269|PubMed:14730579}. 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: Transcriptionally regulated by fur; repressed by iron.
CC       {ECO:0000269|PubMed:12354229}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 8 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA74540.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; Y14084; CAA74540.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL009126; CAB12873.2; -; Genomic_DNA.
DR   PIR; F69831; F69831.
DR   RefSeq; NP_388914.2; NC_000964.3.
DR   RefSeq; WP_003233159.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; C0SP94; -.
DR   SMR; C0SP94; -.
DR   STRING; 224308.BSU10330; -.
DR   PaxDb; C0SP94; -.
DR   PRIDE; C0SP94; -.
DR   EnsemblBacteria; CAB12873; CAB12873; BSU_10330.
DR   GeneID; 936324; -.
DR   KEGG; bsu:BSU10330; -.
DR   PATRIC; fig|224308.179.peg.1111; -.
DR   eggNOG; COG4594; Bacteria.
DR   InParanoid; C0SP94; -.
DR   OMA; RDENFFT; -.
DR   PhylomeDB; C0SP94; -.
DR   BioCyc; BSUB:BSU10330-MON; -.
DR   Proteomes; UP000001570; Chromosome.
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   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; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW   Signal; Transport.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           20..323
FT                   /note="Putative ABC transporter substrate-binding
FT                   lipoprotein YhfQ"
FT                   /id="PRO_0000390292"
FT   DOMAIN          51..322
FT                   /note="Fe/B12 periplasmic-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00344"
FT   LIPID           20
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           20
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   323 AA;  35489 MW;  E3DF94B409E89443 CRC64;
     MKKTLIILTV LLLSVLTAAC SSSSGNQNSK EHKVAVTHDL GKTNVPEHPK RVVVLELGFI
     DTLLDLGITP VGVADDNKAK QLINKDVLKK IDGYTSVGTR SQPSMEKIAS LKPDLIIADT
     TRHKKVYDQL KKIAPTIALN NLNADYQDTI DASLTIAKAV GKEKEMEKKL TAHEEKLSET
     KQKISANSQS VLLIGNTNDT IMARDENFFT SRLLTQVGYR YAISTSGNSD SSNGGDSVNM
     KMTLEQLLKT DPDVIILMTG KTDDLDADGK RPIEKNVLWK KLKAVKNGHV YHVDRAVWSL
     RRSVDGANAI LDELQKEMPA AKK
 
 
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