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 03-AUG-2022, entry version 71.
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}.
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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 AlphaFoldDB; C0SP95; -.
DR SMR; C0SP95; -.
DR STRING; 224308.BSU03950; -.
DR PaxDb; C0SP95; -.
DR PRIDE; C0SP95; -.
DR EnsemblBacteria; CAB12203; CAB12203; BSU_03950.
DR GeneID; 938258; -.
DR KEGG; bsu:BSU03950; -.
DR PATRIC; fig|224308.179.peg.418; -.
DR eggNOG; COG1276; Bacteria.
DR eggNOG; COG2372; Bacteria.
DR InParanoid; C0SP95; -.
DR OMA; MYKGNAT; -.
DR PhylomeDB; C0SP95; -.
DR BioCyc; BSUB:BSU03950-MON; -.
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 Gene3D; 2.60.40.1220; -; 1.
DR InterPro; IPR032694; CopC/D.
DR InterPro; IPR007348; CopC_dom.
DR InterPro; IPR008457; Cu-R_CopD.
DR InterPro; IPR014755; Cu-Rt/internalin_Ig-like.
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;
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 BINDING 24
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT BINDING 110
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
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
