ID I3TJ61_TISMK Unreviewed; 457 AA.
AC I3TJ61;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN Name=aprE {ECO:0000313|EMBL:AFK52799.1};
GN OrderedLocusNames=TMO_0960 {ECO:0000313|EMBL:AFK52799.1};
OS Tistrella mobilis (strain KA081020-065).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC Geminicoccaceae; Tistrella.
OX NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK52799.1, ECO:0000313|Proteomes:UP000005258};
RN [1] {ECO:0000313|EMBL:AFK52799.1, ECO:0000313|Proteomes:UP000005258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK52799.1,
RC ECO:0000313|Proteomes:UP000005258};
RX PubMed=22458477; DOI=10.1021/ja301735a;
RA Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT agents.";
RL J. Am. Chem. Soc. 134:8625-8632(2012).
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}.
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DR EMBL; CP003236; AFK52799.1; -; Genomic_DNA.
DR AlphaFoldDB; I3TJ61; -.
DR STRING; 1110502.TMO_0960; -.
DR KEGG; tmo:TMO_0960; -.
DR eggNOG; COG0845; Bacteria.
DR HOGENOM; CLU_598433_0_0_5; -.
DR Proteomes; UP000005258; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
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 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:UP000005258};
KW Transmembrane {ECO:0000256|RuleBase:RU365093};
KW Transmembrane helix {ECO:0000256|RuleBase:RU365093};
KW Transport {ECO:0000256|RuleBase:RU365093}.
FT TRANSMEM 21..38
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365093"
FT DOMAIN 65..103
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
FT REGION 312..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 235..262
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 339..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..388
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 457 AA; 48715 MW; AAC084DBBC7AE509 CRC64;
MTATTIAPRI DDGAGRPLRT GLIISVLFFG VLGGWAAFAP LDSAAVAPGV VVVENNRQAV
QHRDGGIVAE LPVREGDRVE AGQLLLRLDD TELAAQVSIL SKQIDALKIL EARLVAERDG
LDAIVFPADI TARLGKGEEI DQLVHGQERV FATRTSSRGN QVDILQQRIV QLGAQIKGFE
AQAAANARQL ALIRDELKGT RSLYEKGLTP KTRVLALERA AASLDGERGE NEANAARARQ
AIGEARLQID QIERERQTEV AEQLRQTQEQ LFDLTPRLEA VRAQLGRTEI RAPASGSVVG
LTAFTVGGVI RPGGDGDGDR AQRHAAGGAG PAPPRPDRRC PPGHGRRGAS DRLSLSHHAD
PERQCRADLG RPLHRRAHRR RLLRHAHRGA DHRAAPPARC RPDPGHAGRG DGAAARAHGA
GLSGGAAVAQ HRRHGAGGLI PPRRVACAPQ PAAIVRA
//
