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ARCD_BACSU
ID   ARCD_BACSU              Reviewed;         469 AA.
AC   O32204; Q7B2K7;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Putative arginine/ornithine antiporter {ECO:0000250|UniProtKB:A2RNI5};
GN   Name=yvsH; OrderedLocusNames=BSU33330;
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=9639930; DOI=10.1099/00221287-144-6-1593;
RA   Wipat A., Brignell C.S., Guy J.B., Rose M., Emmerson P.T., Harwood C.R.;
RT   "The yvsA-yvqA (293 degrees - 289 degrees) region of the Bacillus subtilis
RT   chromosome containing genes involved in metal ion uptake and a putative
RT   sigma factor.";
RL   Microbiology 144:1593-1600(1998).
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).
CC   -!- FUNCTION: Catalyzes electroneutral exchange between L-arginine and L-
CC       ornithine. {ECO:0000250|UniProtKB:A2RNI5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginine(out) + L-ornithine(in) = L-arginine(in) + L-
CC         ornithine(out); Xref=Rhea:RHEA:34991, ChEBI:CHEBI:32682,
CC         ChEBI:CHEBI:46911; Evidence={ECO:0000250|UniProtKB:A2RNI5};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC       superfamily. Basic amino acid/polyamine antiporter (APA) (TC 2.A.3.2)
CC       family. {ECO:0000305}.
CC   -!- CAUTION: Has been described as a LysP lysine permease, due in part to
CC       the presence of LYS elements in the regulatory region. {ECO:0000305}.
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DR   EMBL; AJ223978; CAA11718.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15339.1; -; Genomic_DNA.
DR   PIR; D70048; D70048.
DR   RefSeq; NP_391214.1; NC_000964.3.
DR   RefSeq; WP_003244227.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O32204; -.
DR   SMR; O32204; -.
DR   STRING; 224308.BSU33330; -.
DR   TCDB; 2.A.3.2.6; the amino acid-polyamine-organocation (apc) family.
DR   PaxDb; O32204; -.
DR   PRIDE; O32204; -.
DR   EnsemblBacteria; CAB15339; CAB15339; BSU_33330.
DR   GeneID; 936000; -.
DR   KEGG; bsu:BSU33330; -.
DR   PATRIC; fig|224308.179.peg.3618; -.
DR   eggNOG; COG0531; Bacteria.
DR   InParanoid; O32204; -.
DR   OMA; ISTLWAF; -.
DR   PhylomeDB; O32204; -.
DR   BioCyc; BSUB:BSU33330-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   Pfam; PF13520; AA_permease_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid transport; Antiport; Cell membrane; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..469
FT                   /note="Putative arginine/ornithine antiporter"
FT                   /id="PRO_0000360837"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        301..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        347..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        375..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        417..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        439..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   469 AA;  50258 MW;  633FBB1EF2D437F8 CRC64;
     MEQTKKWGFW LLTAFVVGNM VGSGIFSLPS SLASIASPFG ATSAWLLTGA GVLMIALVFG
     HLSIRKPELT AGPQSYARAL FSDPKKGNAA GFTMVWGYWV ASWISNVAII TSLAGYLTSF
     FPILVDKREM FSIGGQEVTL GQLLTFAVCT ILLWGTHAIL VASINGASKL NFVTTLSKVL
     GFVFFIVAGL FVFQTSLFGH FYFPVQGENG TSIGIGGQVH NAAISTLWAF VGIESAVILS
     GRARSQRDVK RATITGLLIA LSIYIIVTLI TMGVLPHDKL VGSEKPFVDV LYAIVGNAGS
     VIMALLAILC LFGTMLGWIL LGSEVPYQAA KAGDFPAFFA KTNKKGSPVI ALIITNVMSQ
     VFIFSVISRT ISDAFTFLTT AATLAYLIPY LVSAIYSLKV VIKGETYDQL KGSRVRDGLI
     AILACAYSVF VIVTGTADLT TFILGIGLFF VGLIVYPFVS NKFQKEKQA
 
 
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