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YCLP_BACSU
ID   YCLP_BACSU              Reviewed;         252 AA.
AC   P94420; Q797P0;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Petrobactin import ATP-binding protein YclP {ECO:0000305};
DE            EC=7.2.2.- {ECO:0000305|PubMed:19955416};
GN   Name=yclP; OrderedLocusNames=BSU03820;
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=8969502; DOI=10.1099/13500872-142-11-3047;
RA   Yamane K., Kumano M., Kurita K.;
RT   "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT   determination of the sequence of a 146 kb segment and identification of 113
RT   genes.";
RL   Microbiology 142:3047-3056(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   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=19955416; DOI=10.1073/pnas.0904793106;
RA   Zawadzka A.M., Kim Y., Maltseva N., Nichiporuk R., Fan Y., Joachimiak A.,
RA   Raymond K.N.;
RT   "Characterization of a Bacillus subtilis transporter for petrobactin, an
RT   anthrax stealth siderophore.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:21854-21859(2009).
CC   -!- FUNCTION: Part of the ABC transporter complex YclNOPQ involved in
CC       uptake of ferric-petrobactin. Petrobactin is a photoreactive 3,4-
CC       catecholate siderophore produced by many members of the B.cereus group,
CC       including B.anthracis. Probably responsible for energy coupling to the
CC       transport system. {ECO:0000269|PubMed:19955416}.
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:19955416};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (YclP),
CC       two transmembrane proteins (YclN and YclO) and a solute-binding protein
CC       (YclQ). {ECO:0000305|PubMed:19955416}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC       protein {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Disruption mutants are unable to use petrobactin
CC       for iron delivery and growth. {ECO:0000269|PubMed:19955416}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; D50453; BAA09014.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12190.1; -; Genomic_DNA.
DR   PIR; D69763; D69763.
DR   RefSeq; NP_388264.1; NC_000964.3.
DR   RefSeq; WP_003234487.1; NZ_JNCM01000031.1.
DR   AlphaFoldDB; P94420; -.
DR   SMR; P94420; -.
DR   STRING; 224308.BSU03820; -.
DR   PaxDb; P94420; -.
DR   PRIDE; P94420; -.
DR   EnsemblBacteria; CAB12190; CAB12190; BSU_03820.
DR   GeneID; 938278; -.
DR   KEGG; bsu:BSU03820; -.
DR   PATRIC; fig|224308.179.peg.405; -.
DR   eggNOG; COG4604; Bacteria.
DR   InParanoid; P94420; -.
DR   OMA; RYAWNGL; -.
DR   PhylomeDB; P94420; -.
DR   BioCyc; BSUB:BSU03820-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 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   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 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..252
FT                   /note="Petrobactin import ATP-binding protein YclP"
FT                   /id="PRO_0000359512"
FT   DOMAIN          2..236
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   252 AA;  28475 MW;  ED2FC0A30F568E65 CRC64;
     MVEVRNVSKQ YGGKVVLEET SVTIQKGKIT SFIGPNGAGK STLLSIMSRL IKKDSGEIYI
     DGQEIGACDS KELAKKMSIL KQANQINIRL TIKDLVSFGR FPYSQGRLTE EDWVHINQAL
     SYMKLEDIQD KYLDQLSGGQ CQRAFIAMVI AQDTDYIFLD EPLNNLDMKH SVEIMKLLKR
     LVEELGKTIV IVIHDINFAS VYSDYIVALK NGRIVKEGPP EEMIETSVLE EIYDMTIPIQ
     TIDNQRIGVY FS
 
 
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