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Database: UniProt
Entry: M1PF05_DESSD
LinkDB: M1PF05_DESSD
Original site: M1PF05_DESSD 
ID   M1PF05_DESSD            Unreviewed;       469 AA.
AC   M1PF05;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Type I secretion membrane fusion protein, HlyD family {ECO:0000313|EMBL:AGF78285.1};
GN   OrderedLocusNames=UWK_01727 {ECO:0000313|EMBL:AGF78285.1};
OS   Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1).
OC   Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC   Desulfocapsaceae; Desulfocapsa.
OX   NCBI_TaxID=1167006 {ECO:0000313|EMBL:AGF78285.1, ECO:0000313|Proteomes:UP000011721};
RN   [1] {ECO:0000313|Proteomes:UP000011721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011721};
RX   PubMed=23961312; DOI=10.4056/sigs.3777412;
RA   Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M., Amann R.,
RA   Schreiber L.;
RT   "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT   deltaproteobacterium specialized in disproportionating inorganic sulfur
RT   compounds.";
RL   Stand. Genomic Sci. 8:58-68(2013).
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; CP003985; AGF78285.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1PF05; -.
DR   STRING; 1167006.UWK_01727; -.
DR   KEGG; dsf:UWK_01727; -.
DR   PATRIC; fig|1167006.5.peg.1906; -.
DR   eggNOG; COG0845; Bacteria.
DR   HOGENOM; CLU_023976_8_0_7; -.
DR   OrthoDB; 9810980at2; -.
DR   Proteomes; UP000011721; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009306; P:protein secretion; 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; 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 membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011721};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        55..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          103..131
FT                   /note="Membrane fusion protein biotin-lipoyl like"
FT                   /evidence="ECO:0000259|Pfam:PF13533"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          179..227
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   469 AA;  52460 MW;  48824E98A26F65DD CRC64;
     MKENSEISKN LKTSHGRTPR SVEKQKKGFF FQQQNSDVDL ITDIRMSLLA QSPRGGSIIL
     WIIVIVFFCA VAWAYVAEVE EVTRASGRVV PARQLQIVQN LEGGILSEIL VNVGDVVKQG
     QLLLRIDEKR FSGPYRESRF NYLALKAQVA RLQSETYSTP FVLPEEVMAE NPEVGNREKE
     LFESRKKELA QTLGVLEEQS RQREQEIVEL EAKIAELSRT RYLLKKEINM TQPLVKGGAV
     SEVEFLRLQR QDSEMQGDIM ASQLALPRAK SRLLEAQKGI TEAKLRFSNN AKKELNDAYA
     KLEGLSATTV ALADRLDRTA VVSPVRGIVN QIFINTVGGV IQPGMNLIEI VPLEDTLLVE
     AKIKPSDIAF LSPNLKATVK FTAYDFTLYG GLEAKVEHIS ADSIVDKQGN SYYLVNVRTT
     KNYLGTKNAP LPIIPGMVAS VDILTGKKRV LTYLMRPILR AQSLALRER
//
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