PHNT_SALPA
ID PHNT_SALPA Reviewed; 369 AA.
AC Q5PFQ7;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Putative 2-aminoethylphosphonate import ATP-binding protein PhnT;
GN Name=phnT; OrderedLocusNames=SPA2295;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
CC -!- FUNCTION: Probably part of the PhnSTUV complex (TC 3.A.1.11.5) involved
CC in 2-aminoethylphosphonate import. Probably responsible for energy
CC coupling to the transport system (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. 2-
CC aminoethylphosphonate importer (TC 3.A.1.11.5) family. {ECO:0000305}.
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DR EMBL; CP000026; AAV78180.1; -; Genomic_DNA.
DR RefSeq; WP_000928782.1; NC_006511.1.
DR AlphaFoldDB; Q5PFQ7; -.
DR SMR; Q5PFQ7; -.
DR EnsemblBacteria; AAV78180; AAV78180; SPA2295.
DR KEGG; spt:SPA2295; -.
DR HOGENOM; CLU_000604_1_1_6; -.
DR OMA; HITAIHV; -.
DR Proteomes; UP000008185; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
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; IPR017662; AminoethylPonate_ABC_PhnT.
DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013611; Transp-assoc_OB_typ2.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF08402; TOBE_2; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50331; SSF50331; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03258; PhnT; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Transport.
FT CHAIN 1..369
FT /note="Putative 2-aminoethylphosphonate import ATP-binding
FT protein PhnT"
FT /id="PRO_0000286740"
FT DOMAIN 19..250
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 51..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 369 AA; 40063 MW; A25659633F9325F3 CRC64;
MLMKTTAAHA PASQGTSGIV LDSLRVAYHG NVVLKPLSLT IEPGEVLALI GPSGSGKTTV
LRAVAGFVQP AGGRILIGDT DVTHLPPYKR GLAMVVQNYA LFPHLKVEDN VAFGLRAQKQ
PKALINERVT QALKTVGMSD YATRYPHQLS GGQQQRVAIA RAIAVRPRVL LLDEPLSALD
AQIRHNMVEE IARLHRELPE LTILYVTHDQ TEALTLADKI GIMKDGSLIA HGETRALYHH
PPNRFAAEFL GRANILSAIA LGITEVPGLV DVSCGGAVIR AFSQGSHHGY NKLLCIRPQH
LSLTPRSAYS NRFNATLQSV HWQGDLTHLL CDVAGETVRM VLTHVNPLPR VGDKLALWFE
PDDAVLIEV