ID   CLPX_AZOBR     STANDARD;      PRT;   422 AA.
AC   P70730; Q9S6M0;
DT   30-MAY-2000 (Rel. 39, Created)
DT   05-JUL-2004 (Rel. 44, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   ATP-dependent Clp protease ATP-binding subunit clpX.
GN   Name=clpX;
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SpF94;
RA   Indorato C., Giannelli L., Bazzicalupo M.;
RT   "Azospirillum brasilense tig-clp-clpx-lon.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 237-422.
RC   STRAIN=SpF94;
RX   MEDLINE=96256595; PubMed=8655539;
RA   Mori E., Fulchieri M., Indorato C., Fani R., Bazzicalupo M.;
RT   "Cloning, nucleotide sequencing, and expression of the Azospirillum
RT   brasilense lon gene: involvement in iron uptake.";
RL   J. Bacteriol. 178:3440-3446(1996).
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   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; AF150957; AAD37436.1; -.
DR   EMBL; U35611; AAB16818.1; -.
DR   PIR; PC6018; PC6018.
DR   HSSP; P32168; 1DO0.
DR   HAMAP; MF_00175; -; 1.
DR   InterPro; IPR003593; AAA_ATPase.
DR   InterPro; IPR003959; AAA_ATPase_centr.
DR   InterPro; IPR004487; ClpX.
DR   InterPro; IPR010603; ZF-C4_ClpX.
DR   SMART; SM00382; AAA; 1.
DR   TIGRFAMs; TIGR00382; clpX; 1.
KW   ATP-binding; Chaperone; Zinc-finger.
FT   ZN_FING      15     40       C4-type.
FT   NP_BIND     118    125       ATP (Potential).
SQ   SEQUENCE   422 AA;  46376 MW;  A497A3A300ECCDFD CRC64;
     MSKSSSGDSK NTLYCSFCGK SQHEVRKLIA GPTVFICDEC VELCMDIIRE ENKTTLVKSR
     DGVPTPRDIH AVLDDYVIGQ HHAKRVLSVA VHNHYKRLAH GTKHNDVELA KSNILLVGPT
     GCGKTLLAQT LARIIDVPFT MADATTLTEA GYVREDVENI ILKLLQAARL QRRAAQRGIV
     YIDEVDKISR KSDNPSITRD VSGEGVQQAL LKIMEGTVAS VPPQGGRKHP QQEFLQVDTS
     NILFICGGAF AGLDKIIAQR GKGTSIGFGA DVRGPDERST GDILREVEPE DLLKFGLIPE
     FIGRLPVVAT LSDLDETALV EILTKPKNAL VKQYQRLFEM EDVRLEFSDD ALRTISHKAI
     QRKTGARGLR SIMESILLDP MFDLPGLSGV ESILVNKEVV EGRAKPLYVH AERRGEQQAP
     GA
//