ID D8G2J0_9CYAN Unreviewed; 587 AA.
AC D8G2J0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Membrane fusion protein biotin-lipoyl like domain-containing protein {ECO:0000259|Pfam:PF13533};
GN ORFNames=OSCI_3200001 {ECO:0000313|EMBL:CBN56830.1};
OS Kamptonema sp. PCC 6506.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Kamptonema.
OX NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN56830.1, ECO:0000313|Proteomes:UP000004532};
RN [1] {ECO:0000313|Proteomes:UP000004532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6506 {ECO:0000313|Proteomes:UP000004532};
RX PubMed=20675499; DOI=10.1128/JB.00704-10;
RA Mejean A., Mazmouz R., Mann S., Calteau A., Medigue C., Ploux O.;
RT "The genome sequence of the cyanobacterium Oscillatoria sp. PCC 6506
RT reveals several gene clusters responsible for the biosynthesis of toxins
RT and secondary metabolites.";
RL J. Bacteriol. 192:5264-5265(2010).
CC -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC family. {ECO:0000256|ARBA:ARBA00009477}.
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DR EMBL; CACA01000285; CBN56830.1; -; Genomic_DNA.
DR RefSeq; WP_007356035.1; NZ_CACA01000285.1.
DR AlphaFoldDB; D8G2J0; -.
DR OrthoDB; 5379451at2; -.
DR Proteomes; UP000004532; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR CDD; cd14688; bZIP_YAP; 1.
DR Gene3D; 2.40.30.170; -; 1.
DR Gene3D; 2.40.420.20; -; 1.
DR Gene3D; 2.40.50.100; -; 2.
DR Gene3D; 1.10.287.470; Helix hairpin bin; 2.
DR InterPro; IPR039562; MFP_biotin_lipoyl_2.
DR InterPro; IPR006143; RND_pump_MFP.
DR NCBIfam; TIGR01730; RND_mfp; 1.
DR PANTHER; PTHR30469; MULTIDRUG RESISTANCE PROTEIN MDTA; 1.
DR PANTHER; PTHR30469:SF36; SLL0180 PROTEIN; 1.
DR Pfam; PF13533; Biotin_lipoyl_2; 1.
DR Pfam; PF13437; HlyD_3; 1.
DR SUPFAM; SSF111369; HlyD-like secretion proteins; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000004532};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 120..167
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 160..206
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 235..310
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 334..380
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 587 AA; 63583 MW; 249E4730D28B0826 CRC64;
MTYSKSPESV VDTEDQQSPT ADTSEIHPTD TDSYQPEDFP PIADRPRPSK PRSRWPLIAT
IAIALGAGFG GWHWWQSSHA RPQQAAATQP QGIPVKLASV ETRSVQDSSE FVSSLEAKRS
VEIKPEIDGL VTEIFVKSGD FVEQGQAIAR IKSDSAQADL RQSQANLIRA QSRLAELQAG
TRPEEIAQAQ AQVAQAQANL AQLRSGSRPE EVGQGQARVS QAEADLADAQ SGSLLEDIAQ
ARAQIEASKA EAELASQQLV RYQALAQEGA ASANTLQEYI QKDRSAKANL REAQRRFEQR
QKNRQAEIER RTGALRQQRE ALRQLQNGSR PEEIARAEAE VAQAKSRLAE LANGTRQEQL
DQAEAQVAEA AAQVRGFEVQ LQETALTAPF AGVIGDVPVK VGYYLQKGDV LTAVTENQLL
DLRLSIPLER MPQLRLGLPV EMLDAQGKAI AKGQISFISP NVSANSQTIL AKATFANPSG
ELLNQQFVKA KVIWQQNPGL LVPVTAVTRL GGQTFVFAAQ KPEQQKPGMP PLIARQKPVK
LGTIDGNNYQ VIEGLQPGEK IVVAGILNLT DGAPIMAQEA GEGEGKN
//
