ID   Q088L9_SHEFN            Unreviewed;       460 AA.
AC   Q088L9;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN   OrderedLocusNames=Sfri_0434 {ECO:0000313|EMBL:ABI70296.1};
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167 {ECO:0000313|EMBL:ABI70296.1, ECO:0000313|Proteomes:UP000000684};
RN   [1] {ECO:0000313|EMBL:ABI70296.1, ECO:0000313|Proteomes:UP000000684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 400 {ECO:0000313|EMBL:ABI70296.1,
RC   ECO:0000313|Proteomes:UP000000684};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA   Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000447; ABI70296.1; -; Genomic_DNA.
DR   RefSeq; WP_011635923.1; NC_008345.1.
DR   AlphaFoldDB; Q088L9; -.
DR   STRING; 318167.Sfri_0434; -.
DR   KEGG; sfr:Sfri_0434; -.
DR   eggNOG; COG0845; Bacteria.
DR   HOGENOM; CLU_023976_8_0_6; -.
DR   OrthoDB; 9775513at2; -.
DR   Proteomes; UP000000684; 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:SF25; MANNURONAN SYNTHASE; 1.
DR   PANTHER; PTHR30386; MEMBRANE FUSION SUBUNIT OF EMRAB-TOLC MULTIDRUG EFFLUX PUMP; 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   Reference proteome {ECO:0000313|Proteomes:UP000000684};
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        30..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365093"
FT   DOMAIN          70..110
FT                   /note="Membrane fusion protein biotin-lipoyl like"
FT                   /evidence="ECO:0000259|Pfam:PF13533"
FT   COILED          169..210
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   460 AA;  51947 MW;  E92E89B2EDF01109 CRC64;
     MSKHLTVADL EMVDDVYGAM MTDAPSGHRL IIWSLAAMMV CFFIWAYFSE LDQVTSGTGK
     VIPSSQIQII QSLDGGILQE IYVQEGGIVT KGQPLARIDD TRFRSDFDQQ EQEVFGLQTN
     IIRMRTELDS IIISDMSSDW RQQVKITKQN LVFPQTIIDE EPELVKRQQE EYSIRLDNLS
     NQLEILVRQI QQRQQEIEEL ASRISTLTTS YQLVSRELEL TRPLARKGIV PEVELLKLER
     TVNDIQGELQ SVRLLRPKVK ASMDEAILKR REAVFVYATD LRAQLNEMQT KLSRMNQAQK
     GAFDKVSKAV IASPVIGTIK KINFNTLGGV VQPGEEIMEI VPSEDKLLIE TKITPKDIAF
     LHPGLPAIVK VTAYDFTRYG GLKGTVEHIS ADTSQDEEGN SFYIVKVRTQ ESSLMKDDGT
     EMPIIPGMLT SVDVITGKKS ILEYILNPIL RAKDTALRER
//