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Database: UniProt
Entry: A0A291GD21_9RHOB
LinkDB: A0A291GD21_9RHOB
Original site: A0A291GD21_9RHOB 
ID   A0A291GD21_9RHOB        Unreviewed;       388 AA.
AC   A0A291GD21;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN   ORFNames=CEW89_10280 {ECO:0000313|EMBL:ATG47916.1};
OS   Celeribacter ethanolicus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Celeribacter.
OX   NCBI_TaxID=1758178 {ECO:0000313|EMBL:ATG47916.1, ECO:0000313|Proteomes:UP000217935};
RN   [1] {ECO:0000313|EMBL:ATG47916.1, ECO:0000313|Proteomes:UP000217935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSPH2 {ECO:0000313|EMBL:ATG47916.1,
RC   ECO:0000313|Proteomes:UP000217935};
RA   Woo J.-H., Kim H.-S.;
RT   "Celeribacter sp. TSPH2 complete genome sequence.";
RL   Submitted (JUN-2017) 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; CP022196; ATG47916.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A291GD21; -.
DR   STRING; 1758178.GCA_001550095_03918; -.
DR   KEGG; ceh:CEW89_10280; -.
DR   OrthoDB; 9810980at2; -.
DR   Proteomes; UP000217935; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009306; P:protein secretion; 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; IPR006144; Secretion_HlyD_CS.
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   PROSITE; PS00543; HLYD_FAMILY; 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};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365093};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217935};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU365093};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU365093};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365093}.
FT   TRANSMEM        16..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365093"
FT   DOMAIN          60..100
FT                   /note="Membrane fusion protein biotin-lipoyl like"
FT                   /evidence="ECO:0000259|Pfam:PF13533"
SQ   SEQUENCE   388 AA;  43324 MW;  C3B54F619FE598A2 CRC64;
     MAFDDVLARD MDRPGWVIKI SALVVLLFLI WAAIARVDEI VRADGQMISS SRPQIVQNLE
     GGILSELLVH EGQEVEQGQV LARLQGTEFR TSADDLQEKL DALEVRRLRL EAEMAGEDAF
     DVPDDLAARV PNVLASEKAL LSARVDDYLA RKDGAMAVLK QAEAERSMME DMLKKNVVAL
     IEVTRARKAH SDAQLKYNEI VTQAELERAE DYSDTLKELA SVKQALTLAQ DQLGRTVITA
     PMRGIVNNLT VTTIGGVIRP GEELVQIIPV DEELFIEAHV RPEDIAHVEP GQEATIKLSA
     YDYTIYGSLK GTVQVVSADT FKDERDPNAQ PYYRVTATVD LDSLTERQQK IEIRPGMRAQ
     VELHTGSKTF LQYLLKPLYK SREAFREP
//
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