PSTB2_NATPD
ID PSTB2_NATPD Reviewed; 284 AA.
AC Q3IQI3;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Phosphate import ATP-binding protein PstB 2 {ECO:0000255|HAMAP-Rule:MF_01702};
DE EC=7.3.2.1 {ECO:0000255|HAMAP-Rule:MF_01702};
DE AltName: Full=ABC phosphate transporter 2 {ECO:0000255|HAMAP-Rule:MF_01702};
DE AltName: Full=Phosphate-transporting ATPase 2 {ECO:0000255|HAMAP-Rule:MF_01702};
GN Name=pstB2 {ECO:0000255|HAMAP-Rule:MF_01702}; Synonyms=abc22a;
GN OrderedLocusNames=NP_3044A;
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC 2260 / Gabara;
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
CC -!- FUNCTION: Part of the ABC transporter complex PstSACB involved in
CC phosphate import. Responsible for energy coupling to the transport
CC system. {ECO:0000255|HAMAP-Rule:MF_01702}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in);
CC Xref=Rhea:RHEA:24440, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.3.2.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01702};
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (PstB),
CC two transmembrane proteins (PstC and PstA) and a solute-binding protein
CC (PstS). {ECO:0000255|HAMAP-Rule:MF_01702}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01702};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01702}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Phosphate
CC importer (TC 3.A.1.7) family. {ECO:0000255|HAMAP-Rule:MF_01702}.
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DR EMBL; CR936257; CAI49613.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3IQI3; -.
DR SMR; Q3IQI3; -.
DR STRING; 348780.NP_3044A; -.
DR EnsemblBacteria; CAI49613; CAI49613; NP_3044A.
DR KEGG; nph:NP_3044A; -.
DR eggNOG; arCOG00923; Archaea.
DR HOGENOM; CLU_000604_1_22_2; -.
DR OMA; PEVMFFD; -.
DR Proteomes; UP000002698; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015415; F:ATPase-coupled phosphate ion transmembrane transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro.
DR CDD; cd03260; ABC_PstB_phosphate_transporter; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005670; Phosp_transpt1.
DR PANTHER; PTHR43423; PTHR43423; 1.
DR Pfam; PF00005; ABC_tran; 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.
DR PROSITE; PS51238; PSTB; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Phosphate transport; Reference proteome; Translocase; Transport.
FT CHAIN 1..284
FT /note="Phosphate import ATP-binding protein PstB 2"
FT /id="PRO_0000272592"
FT DOMAIN 36..278
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01702"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 68..75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01702"
SQ SEQUENCE 284 AA; 30827 MW; 6CB9525693563FEA CRC64;
MTLLSTLRGI SSPARQQPGT QSESRRGGDT LAERGLAVAG VSHGFDGTAV LESVTLAVDR
GETVAIIGPS GTGKTTLLRL LALFSEPDDG TIGLDGTDVW RQSERQRLAA RRRIGMVFQK
ANLFDTTVRR NVRYGLSVRR SWRERLRSWL GGRKRQESVF EALDIVGLAD AASQSASSLS
GGEAQRVAFA RALAYDPDFL LLDEPTSDLD PRNTAVIEEA VDAARSRGLG VAVATHDMHQ
ARRIADRIVV LLDGQVIEAG PTERVFSDPD DARARKFING ELVY
