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ECCB3_MYCTO
ID   ECCB3_MYCTO             Reviewed;         538 AA.
AC   P9WNR2; L0T5Z9; O53688; Q7DA38;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=ESX-3 secretion system ATPase EccB3 {ECO:0000250|UniProtKB:P9WNR3};
DE            EC=3.6.-.- {ECO:0000305};
DE   AltName: Full=ESX conserved component B3 {ECO:0000250|UniProtKB:P9WNR3};
DE   AltName: Full=Type VII secretion system protein EccB3 {ECO:0000250|UniProtKB:P9WNR3};
DE            Short=T7SS protein EccB3 {ECO:0000250|UniProtKB:P9WNR3};
GN   Name=eccB3 {ECO:0000250|UniProtKB:P9WNR3}; OrderedLocusNames=MT0296;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: An ATPase (By similarity). Part of the ESX-3 specialized
CC       secretion system, which is important for iron and zinc uptake or
CC       homeostasis. {ECO:0000250|UniProtKB:P9WNR3,
CC       ECO:0000250|UniProtKB:P9WNR7}.
CC   -!- SUBUNIT: Part of the ESX-3 / type VII secretion system (T7SS), which is
CC       composed of cytosolic and membrane components. The ESX-3 membrane
CC       complex is composed of EccB3, EccC3, EccD3 and EccE3.
CC       {ECO:0000250|UniProtKB:B2HST3}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:B2HST3}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the EccB family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK44520.1; -; Genomic_DNA.
DR   PIR; A70836; A70836.
DR   RefSeq; WP_003401472.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WNR2; -.
DR   SMR; P9WNR2; -.
DR   EnsemblBacteria; AAK44520; AAK44520; MT0296.
DR   KEGG; mtc:MT0296; -.
DR   PATRIC; fig|83331.31.peg.319; -.
DR   HOGENOM; CLU_036302_3_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.50.910; -; 1.
DR   Gene3D; 3.30.2390.20; -; 1.
DR   InterPro; IPR007795; T7SS_EccB.
DR   InterPro; IPR044857; T7SS_EccB_R1.
DR   InterPro; IPR042485; T7SS_EccB_R3.
DR   PANTHER; PTHR40765; PTHR40765; 1.
DR   Pfam; PF05108; T7SS_ESX1_EccB; 1.
DR   TIGRFAMs; TIGR03919; T7SS_EccB; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW   Nucleotide-binding; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..538
FT                   /note="ESX-3 secretion system ATPase EccB3"
FT                   /id="PRO_0000427082"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   538 AA;  55943 MW;  DDE9A080B8E67D03 CRC64;
     MTNQQHDHDF DHDRRSFASR TPVNNNPDKV VYRRGFVTRH QVTGWRFVMR RIAAGIALHD
     TRMLVDPLRT QSRAVLMGVL IVITGLIGSF VFSLIRPNGQ AGSNAVLADR STAALYVRVG
     EQLHPVLNLT SARLIVGRPV SPTTVKSTEL DQFPRGNLIG IPGAPERMVQ NTSTDANWTV
     CDGLNAPSRG GADGVGVTVI AGPLEDTGAR AAALGPGQAV LVDSGAGTWL LWDGKRSPID
     LADHAVTSGL GLGADVPAPR IIASGLFNAI PEAPPLTAPI IPDAGNPASF GVPAPIGAVV
     SSYALKDSGK TISDTVQYYA VLPDGLQQIS PVLAAILRNN NSYGLQQPPR LGADEVAKLP
     VSRVLDTRRY PSEPVSLVDV TRDPVTCAYW SKPVGAATSS LTLLAGSALP VPDAVHTVEL
     VGAGNGGVAT RVALAAGTGY FTQTVGGGPD APGAGSLFWV SDTGVRYGID NEPQGVAGGG
     KAVEALGLNP PPVPIPWSVL SLFVPGPTLS RADALLAHDT LVPDSRPARP VSAEGGYR
 
 
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