ID A0A0D1ECI5_9RHOB Unreviewed; 455 AA.
AC A0A0D1ECI5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN Name=prsE_2 {ECO:0000313|EMBL:KIT15434.1};
GN ORFNames=jaqu_28680 {ECO:0000313|EMBL:KIT15434.1};
OS Jannaschia aquimarina.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=935700 {ECO:0000313|EMBL:KIT15434.1, ECO:0000313|Proteomes:UP000032232};
RN [1] {ECO:0000313|EMBL:KIT15434.1, ECO:0000313|Proteomes:UP000032232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSW-M26 {ECO:0000313|EMBL:KIT15434.1,
RC ECO:0000313|Proteomes:UP000032232};
RA Voget S., Daniel R.;
RT "Genome Sequence of Jannaschia aquimarina DSM28248, a member of the
RT Roseobacter clade.";
RL Submitted (FEB-2015) 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:KIT15434.1}.
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DR EMBL; JYFE01000050; KIT15434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1ECI5; -.
DR STRING; 935700.jaqu_28680; -.
DR PATRIC; fig|935700.4.peg.2968; -.
DR OrthoDB; 9810980at2; -.
DR Proteomes; UP000032232; 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; 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; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|RuleBase:RU365093};
KW Reference proteome {ECO:0000313|Proteomes:UP000032232};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|RuleBase:RU365093};
KW Transmembrane helix {ECO:0000256|RuleBase:RU365093};
KW Transport {ECO:0000256|RuleBase:RU365093}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..455
FT /note="Membrane fusion protein (MFP) family protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002240813"
FT TRANSMEM 37..56
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365093"
FT COILED 181..222
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 283..310
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 455 AA; 50508 MW; 829700E5012705BE CRC64;
MTKLPVKAAT AKVPANRASI PASAASPTSG WSAKRHMTMG IIAMSVLLGG FGTWAATANI
SGAIISQGRV AVEDNRQVVQ HPDGGVVGEI FVREGDRVDE NQILLRLDDT LLRAEAEIVE
DQLRALEARS ARLEAERDNQ DIFEFDQDLL DAAAEDEEIA DAVTGQRNLF DARAESIATQ
TEQLSRRKDQ ISSQIQGIES QREALETQLA FIEEELTAQQ TLLAQGLTQA PRVLSLQREQ
ARLLGQVGEL QAAVAESEGR ITEIDLQIVR LSTDRREQAI AELRDLRVRE VELGERLRAL
EEQLSRLEIT APVAGVVYDL QVFSERSVIR PADPVLYLVP QDRPLVIRSQ VEPIHIDQVF
PGQPVTLRLP AFDARTTPEL AGRVVRVSPD AFIDEATRRA YYSADILPED GEIDRLSQPL
LPGMPVEAYL RTEDRTPIAY LVKPLTDYFN RAFRE
//
