ID A0A2W7NP99_9RHOB Unreviewed; 436 AA.
AC A0A2W7NP99;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN ORFNames=LX81_03330 {ECO:0000313|EMBL:PZX13102.1};
OS Palleronia aestuarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Palleronia.
OX NCBI_TaxID=568105 {ECO:0000313|EMBL:PZX13102.1, ECO:0000313|Proteomes:UP000248916};
RN [1] {ECO:0000313|EMBL:PZX13102.1, ECO:0000313|Proteomes:UP000248916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22009 {ECO:0000313|EMBL:PZX13102.1,
RC ECO:0000313|Proteomes:UP000248916};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (JUN-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:PZX13102.1}.
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DR EMBL; QKZL01000019; PZX13102.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W7NP99; -.
DR OrthoDB; 9810980at2; -.
DR Proteomes; UP000248916; 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.
DR SUPFAM; SSF111369; HlyD-like secretion proteins; 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|RuleBase:RU365093};
KW Reference proteome {ECO:0000313|Proteomes:UP000248916};
KW Transmembrane {ECO:0000256|RuleBase:RU365093};
KW Transmembrane helix {ECO:0000256|RuleBase:RU365093};
KW Transport {ECO:0000256|RuleBase:RU365093}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365093"
FT DOMAIN 65..104
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
FT COILED 160..187
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 212..275
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 436 AA; 47443 MW; 95CAE8378D472CB9 CRC64;
MRYDQIDAAL VHSVGRQVKI ALLVGVLLLG GAGGVAALAQ ISGAVVGMGK LIVEGRWKEI
QHLEGGTVAE IRVAEGDAVE KGQVLFRLDP TTVEARLGII QGQIDTLLAK EARLQAELAG
AADIETSPAL RAAGTPQADA LLRGQADLMR ARAAARAGRE NQLGAQIAQL EEKVVALRAQ
KRAAAQSMEI AAEEVETRQR LSDSNLLRAS DLRDAKRSLA ELQAEDASLD ARILEAREEI
TGRQYERALL DETFREEALT ELDEIRDRLA QLRQEEIGAM DSQRRLSVRA PIGGRLHELS
VHTLGQVVAP GERLVTIIPG DDRLIVEMRL DPQSVDQVYP GQAARLRFTG LDQRTTPQLG
GAVIDISPDA STDEGTGQTF YLARLQIAED ELGRIDGAVL RPGMPLEVFV QTQERSILSY
LVKPMVDQVQ HAMRER
//
