ID CLPX_AZOVI STANDARD; PRT; 440 AA. AC P33683; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 07-MAR-2006, entry version 42. 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 [GENOMIC DNA]. 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 Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M20568; AAA64733.1; -; Genomic_DNA. DR EMBL; M20568; AAA64734.1; ALT_INIT; Genomic_DNA. DR HSSP; P43773; 1OFI. DR HAMAP; MF_00175; -; 1. DR InterPro; IPR013093; AAA_2. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR004487; ClpX. DR InterPro; IPR010603; Znf_C4. DR PANTHER; PTHR11262:SF2; ClpX; 1. DR Pfam; PF07724; AAA_2; 1. DR Pfam; PF06689; zf-C4_ClpX; 1. DR SMART; SM00382; AAA; 1. DR TIGRFAMs; TIGR00382; clpX; 1. KW ATP-binding; Chaperone; Metal-binding; Nucleotide-binding; Zinc; KW Zinc-finger. FT CHAIN 1 440 ATP-dependent Clp protease ATP-binding FT subunit clpX. FT /FTId=PRO_0000160304. 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 //