ID G2FJ51_9GAMM Unreviewed; 443 AA.
AC G2FJ51;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN Name=lktD {ECO:0000313|EMBL:EGW53195.1};
GN ORFNames=TevJSym_bj00230 {ECO:0000313|EMBL:EGW53195.1};
OS endosymbiont of Tevnia jerichonana (vent Tica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=1049564 {ECO:0000313|EMBL:EGW53195.1, ECO:0000313|Proteomes:UP000005167};
RN [1] {ECO:0000313|EMBL:EGW53195.1, ECO:0000313|Proteomes:UP000005167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D.,
RA Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., Hecker M.,
RA Sievert S.M., Schweder T.;
RT "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and Tevnia
RT jerichonana share an identical physiology as revealed by proteogenomic
RT analyses.";
RL ISME J. 0:0-0(2011).
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:EGW53195.1}.
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DR EMBL; AFZB01000036; EGW53195.1; -; Genomic_DNA.
DR RefSeq; WP_006475649.1; NZ_AFZB01000036.1.
DR AlphaFoldDB; G2FJ51; -.
DR PATRIC; fig|1049564.3.peg.2932; -.
DR eggNOG; COG0845; Bacteria.
DR Proteomes; UP000005167; 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; -; 1.
DR InterPro; IPR039562; MFP_biotin_lipoyl_2.
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.
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:UP000005167};
KW Transmembrane {ECO:0000256|RuleBase:RU365093};
KW Transmembrane helix {ECO:0000256|RuleBase:RU365093};
KW Transport {ECO:0000256|RuleBase:RU365093}.
FT TRANSMEM 33..51
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365093"
FT DOMAIN 73..115
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
FT COILED 103..130
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 160..194
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 233..267
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 443 AA; 50083 MW; D7646CF1DB8715B1 CRC64;
MSDTQHYRRS DEQAFLPAAL EVRDTPPSPI GRAISWSLML FFLLAVIWAL IGRVDIVAVA
QGRIIPSGHS KLIQPLESGR VIQIHVTEGQ TVKAGERLIE LDLTTTQAEL ARLRQEAAQL
KQRQRRLQLL SEWIAAPKAH QDPVTAGLSS LESNLLQSQW REYREHLATL KSELARYRAE
RDTLEQQIAK LAATLPLISQ RADDMQTLLK TNAVARHKVL EVEQERISAQ HDLATQRSRR
RELQQAVAEW QAKIRQARSE FQRQTLDQLS EITRQANAIT QEIIKAQVRN YAQTLTAPVD
GVVQQLAIHT IGAIVTPAQE LMRIVPSAEQ LEVEALIENK DIGFVEEGQR AEVKIDAFPF
TKYGTIDAEL TDISNDAVMD ETKGLVFKAR VVLEKTTIQV GKRLVRLTPG MSVTVEAKTG
RRRLIEYFLA PLLKYKQESV RER
//
