(data stored in ACNUC7421 zone)

SWISSPROT: YCNJ_BACSU

ID   YCNJ_BACSU              Reviewed;         541 AA.
AC   C0SP95; P94432; Q797N3;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   11-DEC-2019, entry version 62.
DE   RecName: Full=Copper transport protein YcnJ;
DE   Flags: Precursor;
GN   Name=ycnJ; OrderedLocusNames=BSU03950;
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   SEQUENCE REVISION TO 70.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [4]
RP   FUNCTION IN COPPER UPTAKE, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 21332 / IAM 1213;
RX   PubMed=19168619; DOI=10.1128/jb.01616-08;
RA   Chillappagari S., Miethke M., Trip H., Kuipers O.P., Marahiel M.A.;
RT   "Copper acquisition is mediated by ycnJ and regulated by ycnK and csoR in
RT   Bacillus subtilis.";
RL   J. Bacteriol. 191:2362-2370(2009).
CC   -!- FUNCTION: Involved in uptake of extracellular oxidized copper under
CC       copper-limiting conditions. {ECO:0000269|PubMed:19168619}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- INDUCTION: Highly induced under copper-limiting conditions. Down-
CC       regulated by YcnK, especially under high copper concentrations. Down-
CC       regulated by CsoR. {ECO:0000269|PubMed:19168619}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a growth-defective
CC       phenotype under copper deprivation as well as a reduced intracellular
CC       content of copper. {ECO:0000269|PubMed:19168619}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the CopC family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the CopD family.
CC       {ECO:0000305}.
DR   EMBL; D50453; BAA09026.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12203.2; -; Genomic_DNA.
DR   PIR; F69764; F69764.
DR   RefSeq; NP_388277.2; NC_000964.3.
DR   RefSeq; WP_003246637.1; NZ_JNCM01000031.1.
DR   STRING; 224308.BSU03950; -.
DR   PaxDb; C0SP95; -.
DR   PRIDE; C0SP95; -.
DR   EnsemblBacteria; CAB12203; CAB12203; BSU03950.
DR   GeneID; 938258; -.
DR   KEGG; bsu:BSU03950; -.
DR   PATRIC; fig|224308.179.peg.418; -.
DR   eggNOG; ENOG4108T5E; Bacteria.
DR   eggNOG; COG1276; LUCA.
DR   eggNOG; COG2372; LUCA.
DR   HOGENOM; HOG000051238; -.
DR   InParanoid; C0SP95; -.
DR   KO; K14166; -.
DR   OMA; MYKGNAT; -.
DR   PhylomeDB; C0SP95; -.
DR   BioCyc; BSUB:BSU03950-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0046688; P:response to copper ion; IEA:InterPro.
DR   InterPro; IPR032694; CopC/D.
DR   InterPro; IPR007348; CopC_dom.
DR   InterPro; IPR008457; Cu-R_CopD.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR032693; YtkA-like_dom.
DR   PANTHER; PTHR34820; PTHR34820; 1.
DR   Pfam; PF04234; CopC; 1.
DR   Pfam; PF05425; CopD; 1.
DR   Pfam; PF13115; YtkA; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   1: Evidence at protein level;
DR   PRODOM; C0SP95.
DR   SWISS-2DPAGE; C0SP95.
KW   Cell membrane; Copper; Copper transport; Ion transport; Membrane;
KW   Metal-binding; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..541
FT                   /note="Copper transport protein YcnJ"
FT                   /id="PRO_0000377727"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        262..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        293..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        335..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        370..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        407..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   METAL           24
FT                   /note="Copper"
FT                   /evidence="ECO:0000255"
FT   METAL           110
FT                   /note="Copper"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        70
FT                   /note="V -> L (in Ref. 1; BAA09026)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   541 AA;  59794 MW;  E606581715380959 CRC64;
     MKRNRWWIIL LLFLVFLPKT SFAHAYIVKS SPGENSELKS APAQVEIEFN EPVEEGFHYI
     KVYNSNGDRV DTDKTEIKKD NHHIMTVKLK KNLPKDVYRA EWNAVSADGH PVSGVIPFSI
     GKADGGFSSQ KAADSALNPG TAADRAILYT ALSLFIGTVF FHLFWYKGKS EQLVKRTRRI
     LTGSIAALGL ALLLQLPIQT KANAGGGWGS AFQPGYIRET LFETAGGSIW IIQAALFVLL
     ALSVIPAIRK NRFSSFGYWT APLIFFFGLL LAKAFTGHAA VVEEKTVGIL MDFLHLTSAS
     IWVGGIAALV LLLSKEWRQP DKTLAWETVR RFSPWALTAV GVILFSGLLN GFFIIRSMDS
     LFHTAYGQAL LVKSGLFVFM LVLGAIHFLL TRKQRRTGIS RTLKAEWAIG IAVLITAAVF
     TSLPSPPEPA PEPFYQTKAI ENGQSVSLSI SPNQPGKNVF ELRVTDHNGD PVKNIQQITL
     TVYKTGLSGS ENKSTFTLKE KTKGVFQDQN LSINEKGNWK IKVHGLTGDF NEINIMFTKT
     N
//

If you have problems or comments...

PBIL Back to PBIL home page