ID A0A3L8Q0J1_9GAMM Unreviewed; 460 AA.
AC A0A3L8Q0J1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN ORFNames=D5018_07820 {ECO:0000313|EMBL:RLV60293.1};
OS Parashewanella curva.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Parashewanella.
OX NCBI_TaxID=2338552 {ECO:0000313|EMBL:RLV60293.1, ECO:0000313|Proteomes:UP000281474};
RN [1] {ECO:0000313|EMBL:RLV60293.1, ECO:0000313|Proteomes:UP000281474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C51 {ECO:0000313|EMBL:RLV60293.1,
RC ECO:0000313|Proteomes:UP000281474};
RA Wang G.;
RT "Phylogeny of the Shewanellaceae, and recommendation for two new genera,
RT Pseudoshewanella and Parashewanella.";
RL Submitted (SEP-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}.
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:RLV60293.1}.
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DR EMBL; QZEI01000018; RLV60293.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8Q0J1; -.
DR OrthoDB; 9775513at2; -.
DR Proteomes; UP000281474; Unassembled WGS sequence.
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 Gene3D; 1.10.287.470; Helix hairpin bin; 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 SUPFAM; SSF111369; HlyD-like secretion proteins; 1.
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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365093};
KW Reference proteome {ECO:0000313|Proteomes:UP000281474};
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 30..48
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365093"
FT DOMAIN 68..110
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
FT COILED 169..217
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 460 AA; 51681 MW; EF740A45E389313E CRC64;
MSRKLTSEEL DMVDDVYGAM MTDAPTVHRL IIWSLGAMMI CFLVWSYFSE LDQVTTGVGK
VIPSSQVQII QSLDGGILQE MHVREGMLVT KGQALARIDD TRFRSDYAQQ EQEEFGLKAN
LIRLQAELDS LEVSDVGTDW RKQVNINLKP MVFTQELTEK EPQLIARQQE EYDGRLNNLK
NQIEILARQI QQRQQEMQEL SSKIKTLSTS YQLLTRELEL TKPLAEKGIV PEVELLKLER
GVNDMQGELA GLRILRPKIK AALDEAILKR REAIFVFAAE NRSKMNEWQT KLSRITEAQV
GAKDKVSKAV ITSPVNGTIK TVHINTLGGV VQPGVDIIEI VPSEDQLLIE AKVSPKDIAF
IHPGLPAVVK VTAYDFARYG GLNGTVEHIS ADTTQDEEGN SFYVIRVRTK DSNLKKQDGT
LMPIIPGMLT SVDVITGQRS ILEYILNPIL RARDSALRER
//
