PHNU_SALPA
ID PHNU_SALPA Reviewed; 289 AA.
AC Q5PFQ6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Putative 2-aminoethylphosphonate transport system permease protein PhnU;
GN Name=phnU; OrderedLocusNames=SPA2296;
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; AAV78181.1; -; Genomic_DNA.
DR RefSeq; WP_000052714.1; NC_006511.1.
DR AlphaFoldDB; Q5PFQ6; -.
DR SMR; Q5PFQ6; -.
DR EnsemblBacteria; AAV78181; AAV78181; SPA2296.
DR KEGG; spt:SPA2296; -.
DR HOGENOM; CLU_016047_18_0_6; -.
DR OMA; TPFVMRP; -.
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:0033223; P:2-aminoethylphosphonate transport; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR017636; AminoethylPonate_ABC_perm-PhnU.
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; TIGR03226; PhnU; 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..289
FT /note="Putative 2-aminoethylphosphonate transport system
FT permease protein PhnU"
FT /id="PRO_0000286744"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 68..275
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 289 AA; 31190 MW; 9532F870E81A5DFC CRC64;
MSLILPLEKP ALNLRPLLWL LLPLLVLATL FFWPLSLIVE QALRGANGEI GLETFRQVVD
SKRFVGALLN TLQIAFFATA GCLLLGSVMS LILVFIPFPG SELIGRVVDT FIALPTFLIT
LAFTFIYGSA GLLNGALMSL FAFELPPVDF LYSMQGVILA EITVFTPLVM RPLMAALRQI
DKSQLEAASI LGAHPLRVIG QVIFPAALPA LMAGGSLCLL LTTNEFGIVL FIGAKGVNTL
PMMVYSKAIL ESDYTVACMI ALINIVLSLG LFSLYRLAAS RTGVRSQPC