ID A0A0F2RGK8_9PROT Unreviewed; 463 AA.
AC A0A0F2RGK8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN ORFNames=VR70_11755 {ECO:0000313|EMBL:KJS37714.1};
OS Rhodospirillaceae bacterium BRH_c57.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae.
OX NCBI_TaxID=1629718 {ECO:0000313|EMBL:KJS37714.1, ECO:0000313|Proteomes:UP000033468};
RN [1] {ECO:0000313|EMBL:KJS37714.1, ECO:0000313|Proteomes:UP000033468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c57 {ECO:0000313|EMBL:KJS37714.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-2015) 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:KJS37714.1}.
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DR EMBL; LAEA01000161; KJS37714.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2RGK8; -.
DR STRING; 1629718.VR70_11755; -.
DR PATRIC; fig|1629718.3.peg.1794; -.
DR Proteomes; UP000033468; 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 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; PF13437; HlyD_3; 1.
DR PRINTS; PR01490; RTXTOXIND.
DR SUPFAM; SSF111369; HlyD-like secretion proteins; 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|RuleBase:RU365093};
KW Transmembrane {ECO:0000256|RuleBase:RU365093};
KW Transmembrane helix {ECO:0000256|RuleBase:RU365093};
KW Transport {ECO:0000256|RuleBase:RU365093}.
FT TRANSMEM 31..52
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365093"
FT COILED 227..304
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 463 AA; 50441 MW; BE5412542B8B5FA6 CRC64;
MRSSTLTIPP ITLEGQYEII PNSPFRRLRG LAWAGMAVVA VFIVGFGSWA AVAPLQSAAI
AAGIIEADSS RKTIQHLEGG IIGRILVRDG QYVEAGETLI QLADTRPRTS LASLRGQYLN
AVAREARLMA ERDGHDRVTY PAALTDIRND PVVEQIMAGQ DRILHTRRSL LASRSDLIRQ
RIARVKEEIV GLASQALSAR KQSGLINQEI ADVRVLYKKG LARKPRLLAL ERELAQLEGR
SGEAAAQIAQ AQQVIAESEL NMMTLWNDAQ DEVATALRDT QVQISQLREQ LEAATDIMAR
TEIRAPEAGV VTGLRVRTPG GVIAPGEPLL DLVPANDRLV IKAQIRPDDI DRVRVGLPAQ
VRLTPFKQRL LPPLEGRVSY VSADHRVDER SGQAYYAATI EVEDATLKYD GSALTGKVSG
LVGGPELVPG MPAEIMIQTG ETTVALYALA PILDSFNRAF REN
//
