PUCJ_BACSU
ID PUCJ_BACSU Reviewed; 449 AA.
AC O32139;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Uric acid permease PucJ;
GN Name=pucJ; Synonyms=yunJ; OrderedLocusNames=BSU32430;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP FUNCTION, AND INDUCTION.
RC STRAIN=168;
RX PubMed=11344136; DOI=10.1128/jb.183.11.3293-3302.2001;
RA Schultz A.C., Nygaard P., Saxild H.H.;
RT "Functional analysis of 14 genes that constitute the purine catabolic
RT pathway in Bacillus subtilis and evidence for a novel regulon controlled by
RT the PucR transcription activator.";
RL J. Bacteriol. 183:3293-3302(2001).
RN [3]
RP INDUCTION BY TNRA.
RX PubMed=12823818; DOI=10.1046/j.1365-2958.2003.03567.x;
RA Yoshida K., Yamaguchi H., Kinehara M., Ohki Y.-H., Nakaura Y., Fujita Y.;
RT "Identification of additional TnrA-regulated genes of Bacillus subtilis
RT associated with a TnrA box.";
RL Mol. Microbiol. 49:157-165(2003).
CC -!- FUNCTION: Uptake of uric acid. {ECO:0000269|PubMed:11344136}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Expression is very low in excess nitrogen (glutamate plus
CC ammonia) and is induced by TnrA during limiting-nitrogen conditions
CC (glutamate). Expression is further induced when allantoin or uric acid
CC are added during limiting-nitrogen conditions.
CC {ECO:0000269|PubMed:11344136, ECO:0000269|PubMed:12823818}.
CC -!- SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC
CC 2.A.40) family. {ECO:0000305}.
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DR EMBL; AL009126; CAB15233.1; -; Genomic_DNA.
DR PIR; E70016; E70016.
DR RefSeq; NP_391123.1; NC_000964.3.
DR RefSeq; WP_003243942.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32139; -.
DR SMR; O32139; -.
DR STRING; 224308.BSU32430; -.
DR TCDB; 2.A.40.3.2; the nucleobase/ascorbate transporter (nat) or nucleobase:cation symporter-2 (ncs2) family.
DR PaxDb; O32139; -.
DR DNASU; 937096; -.
DR EnsemblBacteria; CAB15233; CAB15233; BSU_32430.
DR GeneID; 937096; -.
DR KEGG; bsu:BSU32430; -.
DR PATRIC; fig|224308.179.peg.3510; -.
DR eggNOG; COG2233; Bacteria.
DR InParanoid; O32139; -.
DR OMA; PYNTFAQ; -.
DR PhylomeDB; O32139; -.
DR BioCyc; BSUB:BSU32430-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0042907; F:xanthine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042906; P:xanthine transport; IBA:GO_Central.
DR InterPro; IPR006043; NCS2.
DR InterPro; IPR017588; UacT-like.
DR InterPro; IPR006042; Xan_ur_permease.
DR Pfam; PF00860; Xan_ur_permease; 1.
DR TIGRFAMs; TIGR00801; ncs2; 1.
DR TIGRFAMs; TIGR03173; pbuX; 1.
DR PROSITE; PS01116; XANTH_URACIL_PERMASE; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..449
FT /note="Uric acid permease PucJ"
FT /id="PRO_0000165954"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 449 AA; 47100 MW; 9B97CCC42330C087 CRC64;
MKKRSFKVFT LSLQHVLAMY AGAILVPLLV GRALNVTTEQ LSYLLAIDLL TCGVATLLQT
LRGTYIGIGL PVMLGSSFVA VTPMIAIGSN YGIHAIYGSI IAAGVFIFLF ARFFGKLTVL
FPPVVTGTVV TLIGLSLVPT GVKNMAGGEK INGSANPEYG SLENLLLSVG VLVLILVLNR
FLKGFARTLS VLIGIAAGTA AAAIMGKVSF SSVTEAPFFQ IPKPFYFGAP AFEIGPILTM
LIVGIVIIVE STGVFYAIGK ICGRPLTDKD LVKGYRAEGI AILIGGLFNA FPYNTFAQNA
GLLQLTKVKT RNIVVTAGCI LVCLGLIPKI AALASAVPAA VLGGATVVMF GMVIASGVKM
LSTADLKNQY HLLTIACSIA LGIGASTAPG IFAEFPAPIR ILVSDGTITG SLTAIFLNLF
FSLRDKKELT AQQTELPVLE HTLALEKEV
