ID A0A0C1JE42_9RHOB Unreviewed; 436 AA.
AC A0A0C1JE42;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN ORFNames=RA28_08390 {ECO:0000313|EMBL:KIC45712.1};
OS Ruegeria sp. ANG-S4.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1577904 {ECO:0000313|EMBL:KIC45712.1, ECO:0000313|Proteomes:UP000031326};
RN [1] {ECO:0000313|Proteomes:UP000031326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-S4 {ECO:0000313|Proteomes:UP000031326};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(2015).
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:KIC45712.1}.
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DR EMBL; JWLK01000002; KIC45712.1; -; Genomic_DNA.
DR RefSeq; WP_039526661.1; NZ_JWLK01000002.1.
DR AlphaFoldDB; A0A0C1JE42; -.
DR STRING; 1577904.RA28_08390; -.
DR OrthoDB; 9810980at2; -.
DR Proteomes; UP000031326; 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; IPR011053; Single_hybrid_motif.
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; SSF51230; Single hybrid motif; 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:UP000031326};
KW Transmembrane {ECO:0000256|RuleBase:RU365093};
KW Transmembrane helix {ECO:0000256|RuleBase:RU365093};
KW Transport {ECO:0000256|RuleBase:RU365093}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365093"
FT DOMAIN 64..98
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
SQ SEQUENCE 436 AA; 48275 MW; 1542918B384353A0 CRC64;
MSRHPDLDAL AREMRGRPPL RGSLLLGVIL LCIITALIWA ERTELDDVVR VDGRVVPSIN
VQVIEATEPG VVQALHVSEG QIVEAGDLLM ELDTTQIASE LSIEQQRAFG LMARGQRLEA
EITGSALEFA EELVTEAAEV VHSETALFKG RQAELSAEIA ILERQREQRQ REFEESLVDQ
VTAIETLALL AEEHAIMKPL VDQRMEPATT LLALKRNEAE WHGRETRAKA VVRKLQIGLD
EIDDRISATR SRFRSAALTD LAAVTAELSA LRPSLPALRN RAARAQIRSP VRGVINRIHR
TTIGGLARGG EELIEVVPLD DTLLVEAYVR PKDIAFLHVG QPLKVKITAF DFMRYGSLGG
EITRIGADTV ARSERSEEEV FVVEIRTVEA KLGSNERAVE IMPGMITEVD ILSGRKSVLE
YVIQPVLKVK NEALRE
//
