ID Q66AG0_YERPS Unreviewed; 456 AA.
AC Q66AG0;
DT 11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN OrderedLocusNames=YPTB2170 {ECO:0000313|EMBL:CAH21408.1};
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123 {ECO:0000313|EMBL:CAH21408.1, ECO:0000313|Proteomes:UP000001011};
RN [1] {ECO:0000313|EMBL:CAH21408.1, ECO:0000313|Proteomes:UP000001011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953 {ECO:0000313|Proteomes:UP000001011};
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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}.
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DR EMBL; BX936398; CAH21408.1; -; Genomic_DNA.
DR RefSeq; WP_011192461.1; NZ_CP009712.1.
DR AlphaFoldDB; Q66AG0; -.
DR GeneID; 66841397; -.
DR KEGG; ypo:BZ17_293; -.
DR KEGG; yps:YPTB2170; -.
DR PATRIC; fig|273123.14.peg.310; -.
DR Proteomes; UP000001011; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR Gene3D; 2.40.30.170; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR InterPro; IPR039562; MFP_biotin_lipoyl_2.
DR InterPro; IPR006144; Secretion_HlyD_CS.
DR InterPro; IPR010129; T1SS_HlyD.
DR NCBIfam; TIGR01843; type_I_hlyD; 1.
DR PANTHER; PTHR30386; MEMBRANE FUSION SUBUNIT OF EMRAB-TOLC MULTIDRUG EFFLUX PUMP; 1.
DR PANTHER; PTHR30386:SF26; TRANSPORT PROTEIN COMB; 1.
DR Pfam; PF13533; Biotin_lipoyl_2; 1.
DR Pfam; PF13437; HlyD_3; 1.
DR PRINTS; PR01490; RTXTOXIND.
DR SUPFAM; SSF111369; HlyD-like secretion proteins; 1.
DR PROSITE; PS00543; HLYD_FAMILY; 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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365093};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU365093};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU365093};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365093}.
FT TRANSMEM 46..63
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365093"
FT DOMAIN 85..130
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
SQ SEQUENCE 456 AA; 51468 MW; AB55AC6DB9BD733A CRC64;
MSAFIQHIKN RWTRCFTPAR TRDEYDFLPA YLEIVERPIA PLARRTAWLL ILTLLLVLIW
AIIGKLDIHA SASGKVIVAE HSKIIQPAEP GVVTEINVRD GDTVDAGQVL IALNPIGIDA
EVRNINQQLQ YRQLEAARLV ALLADEPLKN FKPPYNSPES LVVASRALLT KEYAEVTAEL
SRQDSELAVN QAHLQAGIEH NSHQKALLKN IHRRLQASRT LAKSKSIAEV ELLVQEREWL
TATAEANRLQ SEQDILRAKA HSLAQTRMHY LAKIDRDNRE RLNKTHEIIH QLQQEQIKMM
DKQRQQTLRA PVAGVIQQLA VHTLGGVVTT AQPLMVLVPE DYQLELDVMI LNKDVGFVLP
GQAVEVKVDS FPYTRFGTLS GEVKHVSRDA MEDQQRGLVF PARIRLLSDT LMVEGKPVRL
SAGMAINAEI KTGRRRVIDY LLSPLQQYQS EAMRER
//
