ID A0A2A2E482_9PSED Unreviewed; 455 AA.
AC A0A2A2E482;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN ORFNames=BZL43_03455 {ECO:0000313|EMBL:PAU61981.1};
OS Pseudomonas sp. PICF141.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1949067 {ECO:0000313|EMBL:PAU61981.1, ECO:0000313|Proteomes:UP000217819};
RN [1] {ECO:0000313|EMBL:PAU61981.1, ECO:0000313|Proteomes:UP000217819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PICF141 {ECO:0000313|EMBL:PAU61981.1,
RC ECO:0000313|Proteomes:UP000217819};
RA Gomez-Lama C., Legarda-Cristobal G., Trivino J.C., Mercado-Blanco J.;
RT "Genome sequences of Pseudomonas strains PIC25, PIC105 and PICF141
RT indigenous of the olive (Olea europaea L.) cv. Picual rhizosphere and
RT effective biological control agents against Verticillium dahliae.";
RL Submitted (JAN-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}.
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:PAU61981.1}.
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DR EMBL; MUNM01000023; PAU61981.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2E482; -.
DR OrthoDB; 9775513at2; -.
DR Proteomes; UP000217819; 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 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365093};
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 40..61
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365093"
FT DOMAIN 81..117
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
FT COILED 251..300
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 455 AA; 50520 MW; DBE1918DCE308DC1 CRC64;
MLLKSGVKDS IRRYFKGSAS LQGQPLPEVN KALIEDAPRV VRLTIWAIIG FFVFLMLWAH
FAVVDEVTKG DGKAIPSSKI QKIQNLEGGI VSELFVTEGQ IVEAGAPLIR LDDTRFASNV
GETEADRLSM LLRVERLSAE VDDRALNFPA DVLKAVPVQA ASEESLYISR RQQLHDEIGG
LKEQLIQRQQ ELREFTSKQS QYRNALSLQR QEINMSEPLV AQGAVSPVEV LRLKRAEVET
RGQLDATTLA IPRAESAIKE VQRKIDETRG KFRSEALTQL NEARTDLNKA QATGKALEDR
VSRTLVTSPV RGIVNKLLVN TIGGVIQPGS DLVEIVPLDD TLLVEAKIRP QDIAFLHPGQ
DATVKFTAYD YTIYGGLKAK LEQIGADTIT DEDKKTTYYI IKLRTERSHL GTDEKPLLII
PGMVASVDII TGKKTVLSYL LKPIIRARAE ALHER
//
