ROCE_BACSU
ID ROCE_BACSU Reviewed; 467 AA.
AC P39137;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Amino-acid permease RocE;
GN Name=rocE {ECO:0000303|PubMed:7540694}; OrderedLocusNames=BSU40330;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=168;
RX PubMed=7540694; DOI=10.1006/jmbi.1995.0342;
RA Gardan R., Rapoport G., Debarbouille M.;
RT "Expression of the rocDEF operon involved in arginine catabolism in
RT Bacillus subtilis.";
RL J. Mol. Biol. 249:843-856(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9205843; DOI=10.1093/dnares/4.2.155;
RA Kasahara Y., Nakai S., Ogasawara N.;
RT "Sequence analysis of the 36-kb region between gntZ and trnY genes of
RT Bacillus subtilis genome.";
RL DNA Res. 4:155-159(1997).
RN [3]
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: Putative transport protein involved in arginine degradative
CC pathway. Probably transports arginine or ornithine.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- INDUCTION: Part of the rocDEF operon. Expression is sigma L dependent,
CC induced by arginine, ornithine or proline.
CC {ECO:0000269|PubMed:7540694}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. Amino acid transporter (AAT) (TC 2.A.3.1) family.
CC {ECO:0000305}.
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DR EMBL; X81802; CAA57399.1; -; Genomic_DNA.
DR EMBL; D78193; BAA11292.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16070.1; -; Genomic_DNA.
DR PIR; S55794; S49268.
DR RefSeq; NP_391913.1; NC_000964.3.
DR RefSeq; WP_003242721.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P39137; -.
DR SMR; P39137; -.
DR STRING; 224308.BSU40330; -.
DR TCDB; 2.A.3.1.11; the amino acid-polyamine-organocation (apc) family.
DR PaxDb; P39137; -.
DR PRIDE; P39137; -.
DR EnsemblBacteria; CAB16070; CAB16070; BSU_40330.
DR GeneID; 937761; -.
DR KEGG; bsu:BSU40330; -.
DR PATRIC; fig|224308.179.peg.4363; -.
DR eggNOG; COG0833; Bacteria.
DR InParanoid; P39137; -.
DR OMA; AMMQCLG; -.
DR PhylomeDB; P39137; -.
DR BioCyc; BSUB:BSU40330-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0006525; P:arginine metabolic process; IDA:UniProtKB.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004840; Amoino_acid_permease_CS.
DR Pfam; PF00324; AA_permease; 1.
DR PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE 2: Evidence at transcript level;
KW Amino-acid transport; Arginine metabolism; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..467
FT /note="Amino-acid permease RocE"
FT /id="PRO_0000054213"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 467 AA; 51634 MW; B1A522C03134E6C2 CRC64;
MNTNQDNGNQ LQRTMKSRHL FMISLGGVIG TGFFLGTGFT INQAGPLGAV LSYLVGGFIM
FLTMLCLGEL AVAFPVSGSF QTYATKFISP AFGFAFGWLY WLGWAVTCAI EFLSAGQLMQ
RWFPHIDVWI WCLVFAALMF ILNAITTKAF AESEFWFSGI KILIILLFII LGGAAMFGLI
DLKGGEQAPF LTHFYEDGLF PNGIKAMLIT MITVNFAFQG TELIGVAAGE SEDPEKTIPR
SIKQTVWRTL VFFVLSIIVI AGMIPWKQAG VVESPFVAVF EQIGIPYAAD IMNFVILIAL
LSVANSGLYA STRILYAMAN EGQAFKALGK TNQRGVPMYS LIVTMAVACL SLLTKFAQAE
TVYMVLLSLA GMSAQVGWIT ISLSQIMFRR KYIREGGKIE DLKFKTPLYP VLPLIGLTLN
TVVLISLAFD PEQRIALYCG VPFMIICYII YHVVIKKRQQ ANRQLEL
