ID A0A257GCC1_9SPHN Unreviewed; 449 AA.
AC A0A257GCC1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN ORFNames=CFE35_07190 {ECO:0000313|EMBL:OYU36043.1};
OS Novosphingobium sp. PASSN1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=2015561 {ECO:0000313|EMBL:OYU36043.1, ECO:0000313|Proteomes:UP000215690};
RN [1] {ECO:0000313|EMBL:OYU36043.1, ECO:0000313|Proteomes:UP000215690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PASSN1 {ECO:0000313|EMBL:OYU36043.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
RL Submitted (JUN-2017) 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}.
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:OYU36043.1}.
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DR EMBL; NKIS01000003; OYU36043.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257GCC1; -.
DR Proteomes; UP000215690; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR Gene3D; 2.40.30.170; -; 1.
DR Gene3D; 2.40.50.100; -; 2.
DR InterPro; IPR039562; MFP_biotin_lipoyl_2.
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; PF13533; Biotin_lipoyl_2; 1.
DR Pfam; PF13437; HlyD_3; 1.
DR PRINTS; PR01490; RTXTOXIND.
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|RuleBase:RU365093};
KW Transmembrane {ECO:0000256|RuleBase:RU365093};
KW Transmembrane helix {ECO:0000256|RuleBase:RU365093};
KW Transport {ECO:0000256|RuleBase:RU365093}.
FT TRANSMEM 35..60
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365093"
FT DOMAIN 74..105
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
FT COILED 174..201
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 226..260
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 449 AA; 49237 MW; C42F38C0556152DE CRC64;
MNMPTTISDP ARQLLPAFGE DGADKAKAPV LLKRLLFTVG GLLIVLFVLA AVIPMGGAVI
GGGAVGVESR VKRIAHPTGG VIKAIYVRNG EHVKQGQLLM RLDDTVTGAD ATYSNLTVEQ
LLAQKGRLEA ERLGSGKLVF PPELTNSANP SAAKAMADEA RLFSIRQTEE AGLRAQLAAR
VLQYNEEIRG LESQMAALKQ QRKLIEPERQ GVKDLWDKQL VTINRLNQLE RTAVDLDGNV
GSLQAQIAQA RARITEAQQQ SIQLGQTRRV QAGTELAQVN TALNQQQLRS VAASDQQDRS
EIRAPYTGVI EKIAFAAMGD VVRPAEPIME IVPDRDTFVV EAMISPTDID QVMKGQPARV
QFSSFNRPTT PEILGRVTYV ATDRTENPEA HQAYYMVRIE VDLAAVKKEG LALRSGMPAE
VFIETGHRSM ISYLTKPFMD QFMRAFRDN
//
