ID A0A1J5N884_9GAMM Unreviewed; 457 AA.
AC A0A1J5N884;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN ORFNames=BM565_03945 {ECO:0000313|EMBL:OIQ47969.1};
OS Gammaproteobacteria bacterium MedPE.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1860093 {ECO:0000313|EMBL:OIQ47969.1, ECO:0000313|Proteomes:UP000182920};
RN [1] {ECO:0000313|EMBL:OIQ47969.1, ECO:0000313|Proteomes:UP000182920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MedPE {ECO:0000313|EMBL:OIQ47969.1};
RX PubMed=27446036; DOI=10.3389/fmicb.2016.00996;
RA Lopez-Perez M., Kimes N.E., Haro-Moreno J.M., Rodriguez-Valera F.;
RT "Not All Particles Are Equal: The Selective Enrichment of Particle-
RT Associated Bacteria from the Mediterranean Sea.";
RL Front. Microbiol. 7:996-996(2016).
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:OIQ47969.1}.
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DR EMBL; MPDF01000016; OIQ47969.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5N884; -.
DR STRING; 1860093.BM565_03945; -.
DR Proteomes; UP000182920; 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 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 28..46
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365093"
FT DOMAIN 66..111
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
FT COILED 173..214
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 457 AA; 51312 MW; 7BCD0996AD66CC99 CRC64;
MKITQQDIEM ADDVYGAMLT EAPSIHRLTI WALAALILTF IIWAYFAALE QVTSGEGKVI
PSSNTQIVQS LDGGILEELY VREGMSVVKG QPIARIDDTR FQSDVNQQKQ EVDSLRANII
RLRAELSSIL VGDDSNWRLQ IKIAKKEVIF TNEFTEKMPE LVARQQQEYN GRLDSLINQL
AIQGRKIEQK KQEIQELDSK VATLQRSYDF ANKELSLTRP LAEKNIIPEV ELLKLERNVN
DILGELEGVQ LLRPKSESSL SETVLQRRET ALKYRTDTRA ELNKMQAELS RMNEAQVGVQ
DKVEKALMTS PVVGTIKTIH INTLGGVITP GQPLMEIVPT QDKLLIEAKI KPQDIAFLHP
GLPAIVKVTA YDFAKYGGLH GKVEHISADT TQDDKGNSFY VIRVRTDSSS IIKKDKTELP
IIPGMMTTVD VITGKRTVLE YILNPVLRAK QSALREQ
//
