ID A0A2A4WKK6_9GAMM Unreviewed; 450 AA.
AC A0A2A4WKK6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN ORFNames=COB33_04855 {ECO:0000313|EMBL:PCI70399.1};
OS Thiotrichaceae bacterium.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae.
OX NCBI_TaxID=2030882 {ECO:0000313|EMBL:PCI70399.1, ECO:0000313|Proteomes:UP000217494};
RN [1] {ECO:0000313|Proteomes:UP000217494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT "A dynamic microbial community with high functional redundancy inhabits the
RT cold, oxic subseafloor aquifer.";
RL Submitted (AUG-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:PCI70399.1}.
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DR EMBL; NVTY01000019; PCI70399.1; -; Genomic_DNA.
DR Proteomes; UP000217494; 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 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 31..49
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365093"
FT DOMAIN 77..115
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 247..296
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 450 AA; 49932 MW; 2735BE21349B64A5 CRC64;
MFKRTNNNHE YEFLPAVLEV QDSPPSPIGR AVIWSVVLLV VITVVWACVG QVDIVATAQG
KIITAGNIKT IQPLEIGVVK EIYVQEGQQV KKGEPLVALD STNSSADKSQ LENELRQARL
AIQXXKVLAT LDFTDRELAY NINQIAAIDG ISDDGMETHR QLLQSEVNGF KFELSSLYNQ
IKSKEAELAA TQNMVVKFEK TLPIVSQRAA SLKNLSDKGL SPELVYLEVE ETRISQEQDL
AAQQHRLAEI GANIKAINDQ ISALTAEIKK ERYTKISELN QKITAIEKEL QKTNNRQQLQ
LLTSPVDGVV NQMEINTIGG IVTPAQPIMT IVPRNKQLEV EAWVANKDIG FVEKGQAAEV
KVEAFPFTKY GVLDAEVVNL SFDAVPDEER GLIYKAKLSL QASVIGTGDK LINLVPGMNV
TVEIKTGKRY LIEYILSPLM QYQDESIKER
//
