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ECCD5_MYCMM
ID   ECCD5_MYCMM             Reviewed;         503 AA.
AC   B2HSU6;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=ESX-5 secretion system protein EccD5 {ECO:0000305};
DE   AltName: Full=ESX conserved component D5 {ECO:0000305};
DE   AltName: Full=Type VII secretion system protein EccD5 {ECO:0000305};
DE            Short=T7SS protein EccD5 {ECO:0000305};
GN   Name=eccD5 {ECO:0000303|PubMed:22925462};
GN   OrderedLocusNames=MMAR_2677 {ECO:0000312|EMBL:ACC41120.1};
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=216594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
RN   [2]
RP   FUNCTION.
RX   PubMed=19602152; DOI=10.1111/j.1365-2958.2009.06783.x;
RA   Abdallah A.M., Verboom T., Weerdenburg E.M., Gey van Pittius N.C.,
RA   Mahasha P.W., Jimenez C., Parra M., Cadieux N., Brennan M.J.,
RA   Appelmelk B.J., Bitter W.;
RT   "PPE and PE_PGRS proteins of Mycobacterium marinum are transported via the
RT   type VII secretion system ESX-5.";
RL   Mol. Microbiol. 73:329-340(2009).
RN   [3]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=22925462; DOI=10.1111/j.1365-2958.2012.08206.x;
RA   Houben E.N., Bestebroer J., Ummels R., Wilson L., Piersma S.R.,
RA   Jimenez C.R., Ottenhoff T.H., Luirink J., Bitter W.;
RT   "Composition of the type VII secretion system membrane complex.";
RL   Mol. Microbiol. 86:472-484(2012).
CC   -!- FUNCTION: Part of the ESX-5 specialized secretion system, which is
CC       responsible for the secretion of EsxN and a number of PE_PGRS and PPE
CC       proteins (PubMed:19602152, PubMed:22925462). This component is
CC       essential for ESX-5 complex stability and secretion (PubMed:22925462).
CC       {ECO:0000269|PubMed:19602152, ECO:0000269|PubMed:22925462}.
CC   -!- SUBUNIT: Part of the ESX-5 / type VII secretion system (T7SS), which is
CC       composed of cytosolic and membrane components. The ESX-5 membrane
CC       complex is composed of EccB5, EccC5, EccD5 and EccE5.
CC       {ECO:0000269|PubMed:22925462}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:22925462}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the EccD/Snm4 family. {ECO:0000305}.
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DR   EMBL; CP000854; ACC41120.1; -; Genomic_DNA.
DR   RefSeq; WP_012394391.1; NC_010612.1.
DR   AlphaFoldDB; B2HSU6; -.
DR   SMR; B2HSU6; -.
DR   STRING; 216594.MMAR_2677; -.
DR   EnsemblBacteria; ACC41120; ACC41120; MMAR_2677.
DR   GeneID; 64261390; -.
DR   KEGG; mmi:MMAR_2677; -.
DR   eggNOG; ENOG502ZAY5; Bacteria.
DR   HOGENOM; CLU_041782_0_0_11; -.
DR   OMA; WIRFIPD; -.
DR   OrthoDB; 1786282at2; -.
DR   Proteomes; UP000001190; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR044049; EccD_transm.
DR   InterPro; IPR006707; T7SS_EccD.
DR   InterPro; IPR024962; YukD-like.
DR   Pfam; PF19053; EccD; 1.
DR   Pfam; PF08817; YukD; 1.
DR   PIRSF; PIRSF017804; Secretion_EccD1; 1.
DR   TIGRFAMs; TIGR03920; T7SS_EccD; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..503
FT                   /note="ESX-5 secretion system protein EccD5"
FT                   /id="PRO_0000434751"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        359..379
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        414..434
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        443..463
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        480..500
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   503 AA;  53516 MW;  49D51B86C72DC2FA CRC64;
     MTAVADAPQA ELEGVSSPRA VVVGIMAGEG VQIGVLLDAN APVSVMTDPL LKVVNSRLRE
     LGESTLEAAG RGRWALCLID GSPLRATQSL TEQDVYDGDR LWIRFIPDTE HRSQVIEHIS
     TAVASNLSKR FASIDPVVAV QVGAGMVGTG VILASGVLGW WRWHHNTWLT TIFASVIAVL
     VLMVAMMLLM RATTDADRRV ADIMLVSGLA PLTVAAASAP PGSVGSPQAV LGFGVLSIAA
     ALALRFTGRR LAIYTAIVTI CGLTTLASLS RMVAATSAVT LFATMLLICV VMYHASPALS
     RRLSGIRLPV FPSATSRWVF EARPDLPTTV AVAAGGPPVL EGPASVRDVV LQAERARSFL
     SGLLVGLGVL MVVSLTSLCN PHTSERWLPL MLAGFTSGFL MLRGRSYVDR WQSITLAVTA
     VIVVAAVSVR YALVLSSPLS VSIVASLLVL LPAAGMTAAA VVPNTIYSPL FRKFVEWTEY
     LCLMPIFPLA FWLMNVYAAI RYR
 
 
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