ID   PHNV_SALPA              Reviewed;         265 AA.
AC   Q5PFQ5;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Putative 2-aminoethylphosphonate transport system permease protein PhnV;
GN   Name=phnV; OrderedLocusNames=SPA2297;
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 the
CC       translocation of the substrate across the membrane (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. {ECO:0000305}.
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DR   EMBL; CP000026; AAV78182.1; -; Genomic_DNA.
DR   RefSeq; WP_000909795.1; NC_006511.1.
DR   AlphaFoldDB; Q5PFQ5; -.
DR   SMR; Q5PFQ5; -.
DR   EnsemblBacteria; AAV78182; AAV78182; SPA2297.
DR   KEGG; spt:SPA2297; -.
DR   HOGENOM; CLU_016047_3_2_6; -.
DR   OMA; LGGTKWI; -.
DR   Proteomes; UP000008185; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   CDD; cd06261; TM_PBP2; 1.
DR   Gene3D; 1.10.3720.10; -; 1.
DR   InterPro; IPR017661; AminoethylPonate_ABC_PhnV.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   SUPFAM; SSF161098; SSF161098; 1.
DR   TIGRFAMs; TIGR03255; PhnV; 1.
DR   PROSITE; PS50928; ABC_TM1; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..265
FT                   /note="Putative 2-aminoethylphosphonate transport system
FT                   permease protein PhnV"
FT                   /id="PRO_0000286748"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          65..253
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   265 AA;  28406 MW;  AAE8264C3523FC22 CRC64;
     MLIWSPKGRA AAGVVASVLF IVFFFLPLAV ILMSSLSQQW NGILPSGFTL NHFVNALHGA
     AWDALLASLT IGFCASLFAL LCGVWAALAL RQYGVKTQKW LSMVFYLPSA IPSVSVGLGI
     LVAFSQGPLQ MNGTLWIVLT AHFVLISAFT FSNVSTGLAR ISADIENVAS SLGASPWYRL
     RHVTLPLLMP WMVSALALSL SLSMGELGAT VMIYPPGWTT LPVAIFSLTD RGNIADGAAL
     TIVLVAITLL LMMKLERIAK RLGQK