ID A0A0F6A500_9GAMM Unreviewed; 445 AA.
AC A0A0F6A500;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN ORFNames=N479_23640 {ECO:0000313|EMBL:KKE81163.1};
OS Pseudoalteromonas luteoviolacea S4054.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1129367 {ECO:0000313|EMBL:KKE81163.1, ECO:0000313|Proteomes:UP000033434};
RN [1] {ECO:0000313|EMBL:KKE81163.1, ECO:0000313|Proteomes:UP000033434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4054 {ECO:0000313|EMBL:KKE81163.1,
RC ECO:0000313|Proteomes:UP000033434};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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:KKE81163.1}.
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DR EMBL; AUXW01000195; KKE81163.1; -; Genomic_DNA.
DR RefSeq; WP_046358332.1; NZ_AUXW01000195.1.
DR AlphaFoldDB; A0A0F6A500; -.
DR PATRIC; fig|1129367.4.peg.5040; -.
DR Proteomes; UP000033434; Unassembled WGS sequence.
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 Gene3D; 1.10.287.470; Helix hairpin bin; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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 29..47
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365093"
FT DOMAIN 67..113
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
FT COILED 200..262
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 445 AA; 49420 MW; D807A3F328B49518 CRC64;
MAKLNKANIE FLPAALEIQA APAPKWARSI VWTLVILLVV TITWLCWGRI DIVASAQGKL
VPQQQVQVIQ PIETGAVLAV HVKEGSEVVE GQILLELDPA ITQADKQDLT AQLNHVNAQV
ERLRELLLFA QQVIDNDEGK IRFVTPKSVH NDTEHNLLLS QIKEFEQSRQ AAWSAIVSLE
AQLMGAQLSV KKIQTMLPLI EERTQSLKVL ENEKLVAREQ YLSLKQEALD LAGQLPIEQA
TVRELKSQIS QAKAQYALLL TDLRKQSLIE LNDALSRQTT LKQQLAKSTF LEGKTRLVAP
VSGTVEALSV TTIGQIVTPA QELMRIVPMN DMLVVDAGLL NKDIGFVFIG QEVEVKIESF
PFTRYGVIEG KVIDVSMDAM EHEVHGLVFP IKVAIEKQSM LIDDRIVALS SGMTVTAEVK
TGYRRIIEFL LSPIIQSVNE GARER
//
