ID A0A429V619_9SPHN Unreviewed; 456 AA.
AC A0A429V619;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN ORFNames=HMF7854_00015 {ECO:0000313|EMBL:RST29393.1};
OS Sphingomonas ginkgonis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=2315330 {ECO:0000313|EMBL:RST29393.1, ECO:0000313|Proteomes:UP000274661};
RN [1] {ECO:0000313|EMBL:RST29393.1, ECO:0000313|Proteomes:UP000274661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMF7854 {ECO:0000313|EMBL:RST29393.1,
RC ECO:0000313|Proteomes:UP000274661};
RA Cha I., Kang H., Kim H., Kang J., Joh K.;
RT "Sphingomonas sp. HMF7854 Genome sequencing and assembly.";
RL Submitted (DEC-2018) 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:RST29393.1}.
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DR EMBL; RWJF01000001; RST29393.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A429V619; -.
DR OrthoDB; 9810980at2; -.
DR Proteomes; UP000274661; 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 Gene3D; 1.10.287.470; Helix hairpin bin; 1.
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.
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}; Membrane {ECO:0000256|RuleBase:RU365093};
KW Reference proteome {ECO:0000313|Proteomes:UP000274661};
KW Transmembrane {ECO:0000256|RuleBase:RU365093};
KW Transmembrane helix {ECO:0000256|RuleBase:RU365093};
KW Transport {ECO:0000256|RuleBase:RU365093}.
FT TRANSMEM 35..54
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365093"
FT DOMAIN 71..105
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
SQ SEQUENCE 456 AA; 49023 MW; 83248E8696B1DD8F CRC64;
MTSISLRSPR LLAPSSVPFV PPSSADSSAE IRLGLIVAFL FFVLFLGWAA VAPLDAAAQA
GGRLAVSGQR QTVQHETGGV VSQILVREGQ HVAQGQVLIR LAGDEARAAE RSLSLQAISL
LAQRERLRAE QAGLTTIARP AEFASLPLED QPAANEAMRI QSVQLASRRS VLQSQQGASR
ARVSEAGSQA SGYRSQFAGI DEQIRLLNQE LAGFYKLESS GFVSKNRIRE MERTRAELIA
QKGQLTASIE QSHGQASESR LQGLEAQSSF MEKTSADLRD VEASLSDVMP KLQAARQQLA
RVEIRAPASG AVVGLAVFTP GGVVSPGQKL LDVVPDRAPL IVETRIPVSD GDDVRNGQAA
YLRFDTLHDR SIGTLAGYVS RVSADAFTDE KTGASFYTAE VVVPLAELQK IEQSPERHNL
RAGIPVSVQL PMRKRTALQY LFEPITGALS GSMHEK
//
