ID A0A345QLZ0_9RHOB Unreviewed; 440 AA.
AC A0A345QLZ0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN ORFNames=C1J03_09990 {ECO:0000313|EMBL:AXI46327.1};
OS Sulfitobacter sp. SK012.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=1389005 {ECO:0000313|EMBL:AXI46327.1, ECO:0000313|Proteomes:UP000253903};
RN [1] {ECO:0000313|EMBL:AXI46327.1, ECO:0000313|Proteomes:UP000253903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK012 {ECO:0000313|EMBL:AXI46327.1,
RC ECO:0000313|Proteomes:UP000253903};
RA Pohlner M., Engelen B., Bunk B.;
RT "Comparative analysis of Sulfitobacter genomes from the North Sea.";
RL Submitted (JAN-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}.
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DR EMBL; CP025804; AXI46327.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345QLZ0; -.
DR KEGG; sulz:C1J03_09990; -.
DR OrthoDB; 9810980at2; -.
DR Proteomes; UP000253903; Chromosome.
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; -; 1.
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: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.
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 Reference proteome {ECO:0000313|Proteomes:UP000253903};
KW Transmembrane {ECO:0000256|RuleBase:RU365093};
KW Transmembrane helix {ECO:0000256|RuleBase:RU365093};
KW Transport {ECO:0000256|RuleBase:RU365093}.
FT TRANSMEM 27..45
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365093"
FT DOMAIN 66..101
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
FT COILED 157..184
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 266..293
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 440 AA; 48337 MW; 9A37251D68540304 CRC64;
MFGNRIEDEF ANNISAAPTA LHDRSSWTLL LAVALGIAAF LFWAATYQIE ETARAVGRVI
PSQQVQIVQS LEGGIVRALM VREGDIVEAG DVLMQIDDIR FTSERGELLE QSSAIAAETT
RLRAEAEFEP KLTFPEELVA RNPQATAVEQ EVFLSRREQL VRELEILEAR LIQKRSALEE
SRAQRDRTRA VLAPLSEEIE LTGGMVDRGV VPKIELLRLQ SRFAELSGDI SVSLAAEPRA
KAAIGEVQGQ IKAARSGYVL AARLRLAKLQ LELAVVQETL RAANDRVKRA ELRAPVLGTI
NTIHMTTLGA VVQPGAALFD IVPIDDSLLI EADLGPRDIA FVRMGERASV KISAYDYLIY
GAMEGEVVRI GADTIKHQDG TEFFRVVIQT DKSYLGTSEN QLPITAGMIA SVDIQTGQKT
VLSYLAKPIL RAKSEALRER
//
