ARTM_BACSU
ID ARTM_BACSU Reviewed; 240 AA.
AC P54537;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Arginine transport ATP-binding protein ArtM;
GN Name=artM; Synonyms=yqiZ; OrderedLocusNames=BSU23960;
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 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(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 FUNCTION IN ARGININE TRANSPORT, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=11423008; DOI=10.1186/gb-2001-2-6-research0019;
RA Sekowska A., Robin S., Daudin J.-J., Henaut A., Danchin A.;
RT "Extracting biological information from DNA arrays: an unexpected link
RT between arginine and methionine metabolism in Bacillus subtilis.";
RL Genome Biol. 2:RESEARCH0019.1-RESEARCH0019.12(2001).
CC -!- FUNCTION: Part of a binding-protein-dependent transport system for
CC arginine. Probably responsible for energy coupling to the transport
CC system. {ECO:0000269|PubMed:11423008}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Impaired growth on arginine as the nitrogen
CC source. {ECO:0000269|PubMed:11423008}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; D84432; BAA12606.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14327.1; -; Genomic_DNA.
DR PIR; H69962; H69962.
DR RefSeq; NP_390276.1; NC_000964.3.
DR RefSeq; WP_004398740.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P54537; -.
DR SMR; P54537; -.
DR STRING; 224308.BSU23960; -.
DR TCDB; 3.A.1.3.15; the atp-binding cassette (abc) superfamily.
DR PaxDb; P54537; -.
DR PRIDE; P54537; -.
DR EnsemblBacteria; CAB14327; CAB14327; BSU_23960.
DR GeneID; 938686; -.
DR KEGG; bsu:BSU23960; -.
DR PATRIC; fig|224308.179.peg.2610; -.
DR eggNOG; COG1126; Bacteria.
DR InParanoid; P54537; -.
DR OMA; EGTTMLM; -.
DR PhylomeDB; P54537; -.
DR BioCyc; BSUB:BSU23960-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015424; F:ABC-type amino acid transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR030679; ABC_ATPase_HisP-typ.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR PIRSF; PIRSF039085; ABC_ATPase_HisP; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Transport.
FT CHAIN 1..240
FT /note="Arginine transport ATP-binding protein ArtM"
FT /id="PRO_0000093144"
FT DOMAIN 2..236
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 240 AA; 26950 MW; B559DA39D6C3BAA8 CRC64;
MIKVEKLSKS FGKHEVLKNI STTIAEGEVV AVIGPSGSGK STFLRCLNLL EKPNGGTITI
KDTEITKPKT NTLKVRENIG MVFQHFHLFP HKTVLENIMY APVNVKKESK QAAQEKAEDL
LRKVGLFEKR NDYPNRLSGG QKQRVAIARA LAMNPDIMLF DEPTSALDPE MVKEVLQVMK
ELVETGMTMV IVTHEMGFAK EVADRVLFMD QGMIVEDGNP KEFFMSPKSK RAQDFLEKIL