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ECCA5_MYCMM
ID   ECCA5_MYCMM             Reviewed;         610 AA.
AC   B2HSU9;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=ESX-5 secretion system protein EccA5 {ECO:0000305};
DE   AltName: Full=ESX conserved component A5 {ECO:0000305};
DE   AltName: Full=Type VII secretion system protein EccA5 {ECO:0000305};
DE            Short=T7SS protein EccA5 {ECO:0000305};
GN   Name=eccA5 {ECO:0000303|PubMed:22925462};
GN   OrderedLocusNames=MMAR_2680 {ECO:0000312|EMBL:ACC41123.1};
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, 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). EccA5 exhibits ATPase
CC       activity and may provide energy for the export of ESX-5 substrates (By
CC       similarity). {ECO:0000250|UniProtKB:P9WPH9,
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.
CC       {ECO:0000250|UniProtKB:P9WPH9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22925462}.
CC   -!- SIMILARITY: Belongs to the CbxX/CfxQ family. {ECO:0000305}.
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DR   EMBL; CP000854; ACC41123.1; -; Genomic_DNA.
DR   RefSeq; WP_012394394.1; NC_010612.1.
DR   AlphaFoldDB; B2HSU9; -.
DR   SMR; B2HSU9; -.
DR   STRING; 216594.MMAR_2680; -.
DR   EnsemblBacteria; ACC41123; ACC41123; MMAR_2680.
DR   KEGG; mmi:MMAR_2680; -.
DR   eggNOG; COG0457; Bacteria.
DR   eggNOG; COG0464; Bacteria.
DR   HOGENOM; CLU_008749_5_0_11; -.
DR   OMA; RTGRWPD; -.
DR   OrthoDB; 1115436at2; -.
DR   Proteomes; UP000001190; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 1.25.40.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041627; AAA_lid_6.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR000641; CbxX/CfxQ.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR023835; T7SS_EccA.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17866; AAA_lid_6; 1.
DR   PRINTS; PR00819; CBXCFQXSUPER.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR03922; T7SS_EccA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..610
FT                   /note="ESX-5 secretion system protein EccA5"
FT                   /id="PRO_0000434748"
FT   BINDING         357..364
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   610 AA;  67673 MW;  6C1408F34B0B967B CRC64;
     MTRAQSAADD ARNAMVAGLL ASGISVNGLQ PSHNPQVAAK MFTTATKLDP AMCDAWLARL
     LAGDQTMDVL AGAWAAVRTF GWETRRLGVT DLQFRPEVSD GLFLRLAVTS VDSLACAYAA
     VLAENKRYQE ASDLLDTTDP KHPFDAELVS YVRGVLYFRT KRWPDVLAQF PEATPWRHPE
     LKAAGAAMAT TALASLGVFE EAFRRAQEAI EGDRVPGAAN IALYTQGMCL RHVGREEEAV
     ELLRRVYSRD AKFSPAREAL DNPNYRLVLT DPETIEARKD PWDPDSAPTR AQTEAARHAE
     MAAKYLAEGD AELNAMLGME QAKKEIKLIK STTKVNLARA KMGLPVPVTS RHTLLLGPPG
     TGKTSVARAF TKQLCGLTVL RKPLVVETSR TKLLGRYMAD AEKNTEEMLE GSLGGAVFFD
     EMHTLHEKGY SQGDPYGNAI INTLLLYMEN HRDELVVFGA GYAKAMEKML EVNQGLRRRF
     STVIEFFSYT PEELIALTKL MGQENEDVIT EEEAQVLLPS YTRFYNDQNY SEDGDLIRGI
     DMLGNAGFVR NVVEKARDHR SFRLDDEDLD AVLNSDLTEF SELQMRRFRE LTKEDLAEGL
     SAAVAEKKTN
 
 
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