ID ARTP_BACSU Reviewed; 255 AA.
AC P54535;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 27-MAR-2024, entry version 136.
DE RecName: Full=Arginine-binding extracellular protein ArtP;
DE Flags: Precursor;
GN Name=artP; Synonyms=yqiX; OrderedLocusNames=BSU23980;
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 / 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. {ECO:0000269|PubMed:11423008}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Cells show impaired growth on arginine as the
CC nitrogen source. {ECO:0000269|PubMed:11423008}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 family.
CC {ECO:0000305}.
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DR EMBL; D84432; BAA12604.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14329.1; -; Genomic_DNA.
DR PIR; F69962; F69962.
DR RefSeq; NP_390278.1; NC_000964.3.
DR RefSeq; WP_004398706.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P54535; -.
DR SMR; P54535; -.
DR STRING; 224308.BSU23980; -.
DR TCDB; 3.A.1.3.15; the atp-binding cassette (abc) superfamily.
DR PaxDb; 224308-BSU23980; -.
DR EnsemblBacteria; CAB14329; CAB14329; BSU_23980.
DR GeneID; 938682; -.
DR KEGG; bsu:BSU23980; -.
DR PATRIC; fig|224308.179.peg.2612; -.
DR eggNOG; COG0834; Bacteria.
DR InParanoid; P54535; -.
DR OrthoDB; 9811552at2; -.
DR PhylomeDB; P54535; -.
DR BioCyc; BSUB:BSU23980-MONOMER; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR CDD; cd13628; PBP2_Ala; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR001320; Iontro_rcpt_C.
DR InterPro; IPR018313; SBP_3_CS.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR PANTHER; PTHR35936:SF19; ABC TRANSPORTER ARGININE-BINDING PROTEIN ARTJ-RELATED; 1.
DR PANTHER; PTHR35936; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE F; 1.
DR Pfam; PF00497; SBP_bac_3; 1.
DR SMART; SM00062; PBPb; 1.
DR SMART; SM00079; PBPe; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS01039; SBP_BACTERIAL_3; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 20..255
FT /note="Arginine-binding extracellular protein ArtP"
FT /id="PRO_0000031779"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 255 AA; 28312 MW; 7ABD32FCE9027A30 CRC64;
MKKWLLLLVA ACITFALTAC GSSNSGSESG KKKLIMGTSA DYKPFEYKEG DNIVGFDVEL
AKALAKKAGY EIEVQDMDFN SLITALKSKQ VDLVLSGMTP TPERKKQVDF SDVYYTANHM
IVSKKDSGIQ SLKDLKGKTV GVQLGSIQEE KGKELSPEYG FKTEDRNRIS DLVQEIKSDR
FDAAIIEDIV AEGYFKSNDD LQGFVIPDAK AEEAGSAIAF RKDSELTDKF NKALKEMEDN
GELEKLKKKW FTGEK
//
