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 27-MAR-2024, entry version 126.
DE RecName: Full=Putative arginine/ornithine antiporter {ECO:0000250|UniProtKB:A2RNI5};
GN Name=yvsH; OrderedLocusNames=BSU33330;
OS Bacillus subtilis (strain 168).
OC Bacteria; Bacillota; 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; 224308-BSU33330; -.
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 OrthoDB; 9762947at2; -.
DR PhylomeDB; O32204; -.
DR BioCyc; BSUB:BSU33330-MONOMER; -.
DR Proteomes; UP000001570; Chromosome.
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 Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR InterPro; IPR002293; AA/rel_permease1.
DR PANTHER; PTHR42770; AMINO ACID TRANSPORTER-RELATED; 1.
DR PANTHER; PTHR42770:SF14; ARGININE_ORNITHINE ANTIPORTER-RELATED; 1.
DR Pfam; PF13520; AA_permease_2; 1.
DR PIRSF; PIRSF006060; AA_transporter; 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
//
