ID   CLPX_AZOVI     STANDARD;      PRT;   440 AA.
AC   P33683;
DT   01-FEB-1994 (Rel. 28, Created)
DT   01-FEB-1994 (Rel. 28, 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   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=89123097; PubMed=2644218;
RA   Jacobson M.R., Brigle K.E., Bennett L.T., Setterquist R.A.,
RA   Wilson M.S., Cash V.L., Beynon J., Newton W.E., Dean D.R.;
RT   "Physical and genetic map of the major nif gene cluster from
RT   Azotobacter vinelandii.";
RL   J. Bacteriol. 171:1017-1027(1989).
RN   [2]
RP   SIMILARITY TO CLPX.
RX   MEDLINE=94043020; PubMed=8226770;
RA   Gottesman S., Clark W.P., de Crecy-Lagard V., Maurizi M.R.;
RT   "ClpX, an alternative subunit for the ATP-dependent Clp protease of
RT   Escherichia coli. Sequence and in vivo activities.";
RL   J. Biol. Chem. 268:22618-22626(1993).
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; M20568; AAA64733.1; -.
DR   EMBL; M20568; AAA64734.1; ALT_INIT.
DR   HSSP; P43773; 1OFI.
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   Pfam; PF00004; AAA; 1.
DR   Pfam; PF06689; zf-C4_ClpX; 1.
DR   SMART; SM00382; AAA; 1.
DR   TIGRFAMs; TIGR00382; clpX; 1.
KW   ATP-binding; Chaperone; Zinc-finger.
FT   ZN_FING       9     34       C4-type.
FT   NP_BIND     119    126       ATP (Potential).
SQ   SEQUENCE   440 AA;  47983 MW;  CBB2093FA8C80D09 CRC64;
     MDKTDKPCCS FCGAEKSPTV PLIAGNDGRI CEACVKLAHQ VVSSWGQRRK NQQLAPQLRT
     PVEYKKHLDE SVIGQEAAKE TLSVAVYNHY LRLLNCDREP VCQLGEQVEL EKSNILMAGP
     SGTGKTLLVR TLARILGVPF AMADATTLTQ AGYVGDDVDS IITRLLDAAG GDVQQAQWGI
     VYIDEVDKLA KRSGGGTAVR DISGEGVQQA LLKMVEGTEV RISKSGRRNE HSEEQVVDTR
     NILFIAGGAF PGLEALVSSR IQPKNTGIGF HAQPRREAPS INELMASLLP DDLHEFGLIP
     EFIGRFPIIT FLQELDHATL LRILTEPRNA LVKQYKQLFA YQGVELVITD AALNYIADQA
     LIRKTGARGL RAVLEAALQQ TMFNMPSQPQ LRGCTLDLVE HEDGGRSLEV LTRLAEDGSG
     RIQPDPSPVV EEKSALSADL
//