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Database: UniProt
Entry: F3FP65_PSESX
LinkDB: F3FP65_PSESX
Original site: F3FP65_PSESX 
ID   F3FP65_PSESX            Unreviewed;       445 AA.
AC   F3FP65;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN   ORFNames=PSYJA_24793 {ECO:0000313|EMBL:EGH32007.1};
OS   Pseudomonas syringae pv. japonica str. M301072.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=629262 {ECO:0000313|EMBL:EGH32007.1, ECO:0000313|Proteomes:UP000004471};
RN   [1] {ECO:0000313|EMBL:EGH32007.1, ECO:0000313|Proteomes:UP000004471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M301072PT {ECO:0000313|Proteomes:UP000004471};
RX   PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA   Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA   Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT   "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT   genomics of 19 Pseudomonas syringae isolates.";
RL   PLoS Pathog. 7:E1002132-e1002132(2011).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|RuleBase:RU365093}; Single-pass membrane protein
CC       {ECO:0000256|RuleBase:RU365093}.
CC   -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC       family. {ECO:0000256|ARBA:ARBA00009477, ECO:0000256|RuleBase:RU365093}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGH32007.1}.
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DR   EMBL; AEAH01001118; EGH32007.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3FP65; -.
DR   PATRIC; fig|629262.5.peg.4122; -.
DR   HOGENOM; CLU_023976_1_1_6; -.
DR   Proteomes; UP000004471; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IEA:InterPro.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 1.10.287.470; Helix hairpin bin; 1.
DR   InterPro; IPR043602; CusB_dom_1.
DR   InterPro; IPR010129; T1SS_HlyD.
DR   NCBIfam; TIGR01843; type_I_hlyD; 1.
DR   PANTHER; PTHR30386:SF17; ALKALINE PROTEASE SECRETION PROTEIN APRE; 1.
DR   PANTHER; PTHR30386; MEMBRANE FUSION SUBUNIT OF EMRAB-TOLC MULTIDRUG EFFLUX PUMP; 1.
DR   Pfam; PF00529; CusB_dom_1; 1.
DR   PRINTS; PR01490; RTXTOXIND.
DR   SUPFAM; SSF111369; HlyD-like secretion proteins; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|RuleBase:RU365093};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU365093}; Membrane {ECO:0000256|RuleBase:RU365093};
KW   Transmembrane {ECO:0000256|RuleBase:RU365093};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU365093};
KW   Transport {ECO:0000256|RuleBase:RU365093}.
FT   TRANSMEM        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365093"
FT   DOMAIN          33..398
FT                   /note="Cation efflux system protein CusB"
FT                   /evidence="ECO:0000259|Pfam:PF00529"
SQ   SEQUENCE   445 AA;  48721 MW;  AAD770DE6BFA0B6A CRC64;
     MNSPIDTHYA VPGKERGVQF FVRAGWILML AGAGSFFLWA SLAPLDQGIA VQGTVVVSGK
     RKAVQSLDGG VVSKILVSEG QLVKEGEPLF RLDQTQVEAD VQSLRAQYRM AWASLARWQS
     ERDNLDEVRF PAELIAAGQG QDPDPRLALV LEGQRQLFSS RRQALAREQS GLQASIEGAG
     MQLAGMRRAR SDLLAQADSL RKQLSNLEPL AQNGFIPGNR LLEFQRQLSQ VQQSLAQNAG
     ETGRIEQGIV ESRLRLQQQR EEYQKEVRSQ WADAQVKALT LEQQLASAGF SLQHSAILAP
     ADGIAVNLGV HTEGAVVRAG ETLLEIVPQG TRLEVEGRLP VQLIDKVASH LPVDILFTAF
     NQSRTPRVSG EVSLISADQM QDEKTGQPYY VLRTSVGDAA LEKLNGLVIK PGMPAEMFVR
     TGERSLLNYL FKPLLDRAGS ALTEE
//
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