(data stored in SCRATCH zone)

HOGENOM: ACIF5_1_PE1012

ID   ACIF5_1_PE1012                       STANDARD;      PRT;   423 AA.
AC   ACIF5_1_PE1012; B5EQ29;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX;
DE   (ACIF5_1.PE1012).
GN   Name=clpX; OrderedLocusNames=Lferr_1032;
OS   ACIDITHIOBACILLUS FERROOXIDANS ATCC 53993.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=380394;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACIF5_1.PE1012.
CC       Acidithiobacillus ferrooxidans ATCC 53993 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:CLPX_ACIF5
CC   -!- FUNCTION: ATP-dependent specificity component of the Clp protease.
CC       It directs the protease to specific substrates. Can perform
CC       chaperone functions in the absence of ClpP (By similarity).
CC   -!- SUBUNIT: Heterodimer of ClpP and ClpX (By similarity).
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family.
CC   -!- GENE_FAMILY: HOG000010093 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B5EQ29; -.
DR   EMBL; CP001132; ACH83274.1; -; Genomic_DNA.
DR   RefSeq; YP_002219481.1; NC_011206.1.
DR   STRING; B5EQ29; -.
DR   GeneID; 6877001; -.
DR   GenomeReviews; CP001132_GR; Lferr_1032.
DR   KEGG; afe:Lferr_1032; -.
DR   OMA; DCIQIDT; -.
DR   ProtClustDB; CLSK2407754; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   HAMAP; MF_00175; ClpX; 1; -.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR013093; ATPase_AAA-2.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR   InterPro; IPR010603; Znf_C4.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   Pfam; PF06689; zf-C4_ClpX; 1.
DR   SMART; SM00382; AAA; 1.
DR   TIGRFAMs; TIGR00382; ClpX; 1.
DR   HOGENOMDNA; ACIF5_1.PE1012; -.
KW   ATP-binding; Chaperone; Complete proteome; Metal-binding;
KW   Nucleotide-binding; Zinc; Zinc-finger.
SQ   SEQUENCE   423 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAGKHEGSGE KTLYCSFCGK SQHEVRKLIA GPSVFICDEC IELCNDIVKD EILDDHSEAQ
     DKLPKPMEIR KTLDDYVIGQ DVAKKVLSVA VYNHYKRLEH GGKDNEVELD KSNILLIGPT
     GSGKTLLAQT LARLLNVPFA MADATTLTEA GYVGEDVENI IQKLLQKCDY DVEKAQTGIV
     YIDEIDKITR KSENPSITRD VSGEGVQQAL LKLIEGTVAS VPPQGGRKHP QQEFLQVDTR
     HILFICGGAF AGLEKSVSAR LEKGGMGFNA PLKRRDKEAT AAMLMQNLEP EDLVRYGLIP
     EFVGRLPILA LLEELDEEAL ISILTDPKNA LVKQYQKLFA LEGVTLEFRT EALRAIAKKA
     LARKTGARGL RSILEQILLD TMYELPSMSG VKKVVVDAAV VESGTKPLLV YDDAAKVDMS
     HPA
//

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