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Database: UniProt
Entry: I9L7G4_9SPHN
LinkDB: I9L7G4_9SPHN
Original site: I9L7G4_9SPHN 
ID   I9L7G4_9SPHN            Unreviewed;       458 AA.
AC   I9L7G4;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN   ORFNames=WSK_0917 {ECO:0000313|EMBL:EIZ80359.1};
OS   Novosphingobium sp. Rr 2-17.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=555793 {ECO:0000313|EMBL:EIZ80359.1, ECO:0000313|Proteomes:UP000004732};
RN   [1] {ECO:0000313|EMBL:EIZ80359.1, ECO:0000313|Proteomes:UP000004732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RR2-17 {ECO:0000313|Proteomes:UP000004732};
RX   PubMed=22933764; DOI=10.1128/JB.01159-12;
RA   Gan H.M., Chew T.H., Hudson A.O., Savka M.A.;
RT   "Genome Sequence of Novosphingobium sp. Strain Rr 2-17, a Nopaline Crown
RT   Gall-Associated Bacterium Isolated from Vitis vinifera L. Grapevine.";
RL   J. Bacteriol. 194:5137-5138(2012).
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:EIZ80359.1}.
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DR   EMBL; AKFJ01000012; EIZ80359.1; -; Genomic_DNA.
DR   RefSeq; WP_008993874.1; NZ_AKFJ01000012.1.
DR   AlphaFoldDB; I9L7G4; -.
DR   PATRIC; fig|555793.3.peg.919; -.
DR   eggNOG; COG0845; Bacteria.
DR   OrthoDB; 9810980at2; -.
DR   Proteomes; UP000004732; 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: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.
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:UP000004732};
KW   Transmembrane {ECO:0000256|RuleBase:RU365093};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU365093};
KW   Transport {ECO:0000256|RuleBase:RU365093}.
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365093"
FT   DOMAIN          79..102
FT                   /note="Membrane fusion protein biotin-lipoyl like"
FT                   /evidence="ECO:0000259|Pfam:PF13533"
SQ   SEQUENCE   458 AA;  49787 MW;  63E9E4DF549B37CD CRC64;
     MASGVITVPH RLVGSLADMD YAGEEGVAAR ESGLGWVVVA LFFGGFIGFS AFVRLDAAAH
     AEGNVSVAGN RQAVQHRDGG VVQALHVQEG QFVRAGDVLI ELAGAEVVAN ERAQASQVIN
     LQAERARLLA ERARSAVIAE PVSFARLDSQ DRVLAQQAMA LQNAILASQR RSVVAQKDVL
     SQQAAQLRQR ITGIGEQLTE NEKQRDLFDQ QLKGMTTLVD KGYVSVNRVR ELERARAGVS
     SDRANLSASG ASAREQIGEI RMQGLTIDAK TLADVAQDLR TNEQSLGEAL PKWEALKRQS
     EETRIRAPAT GQVVGLRVFT VGGVISAGTT LMEIVPDQVP LVIEARFSPD DADDMHVGQK
     AEARFPTMHE RDLPVFSGTL TRFSADAFTD EHTGLRYYTG EVTVPAKALD EIKRRKGPDE
     GLRPGLPVDV LIPLKKRTVL QYLLEPLNQA IWRSGREH
//
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