(data stored in ACNUC29543 zone)

SWISSPROT: CLPX_ACIBT

ID   CLPX_ACIBT              Reviewed;         437 AA.
AC   A3M1Y8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   08-MAY-2019, entry version 80.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000255|HAMAP-Rule:MF_00175};
GN   Name=clpX {ECO:0000255|HAMAP-Rule:MF_00175};
GN   OrderedLocusNames=A1S_0477;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 /
OS   NCDC KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by
RT   high-density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00175}.
CC   -!- SUBUNIT: Component of the ClpX-ClpP complex. Forms a hexameric
CC       ring that, in the presence of ATP, binds to fourteen ClpP subunits
CC       assembled into a disk-like structure with a central cavity,
CC       resembling the structure of eukaryotic proteasomes.
CC       {ECO:0000255|HAMAP-Rule:MF_00175}.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family.
CC       {ECO:0000255|HAMAP-Rule:MF_00175}.
DR   EMBL; CP000521; ABO10932.2; -; Genomic_DNA.
DR   SMR; A3M1Y8; -.
DR   EnsemblBacteria; ABO10932; ABO10932; A1S_0477.
DR   KEGG; acb:A1S_0477; -.
DR   HOGENOM; HOG000010093; -.
DR   KO; K03544; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.50.30; -; 1.
DR   HAMAP; MF_00175; ClpX; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010603; Znf_CppX_C4.
DR   InterPro; IPR038366; Znf_CppX_C4_sf.
DR   PANTHER; PTHR11262; PTHR11262; 1.
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   SMART; SM01086; ClpB_D2-small; 1.
DR   SMART; SM00994; zf-C4_ClpX; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00382; clpX; 1.
PE   3: Inferred from homology;
DR   PRODOM; A3M1Y8.
DR   SWISS-2DPAGE; A3M1Y8.
KW   ATP-binding; Chaperone; Metal-binding; Nucleotide-binding; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    437       ATP-dependent Clp protease ATP-binding
FT                                subunit ClpX.
FT                                /FTId=PRO_1000097918.
FT   ZN_FING      11     36       C4-type. {ECO:0000255|HAMAP-
FT                                Rule:MF_00175}.
FT   NP_BIND     119    126       ATP. {ECO:0000255|HAMAP-Rule:MF_00175}.
SQ   SEQUENCE   437 AA;  48083 MW;  3A78784709BB089D CRC64;
     MSEHPQGQKH CSFCGKTQSE VGKLIAGEDA YICNECVDVC LDLVQTSQQV EAGDWASKAL
     PKPHEIRAAL DQYVIGQDLA KKTLSVAVYN HYKRLKVGQS GHVSKDVEIA KSNILLIGPT
     GSGKTLLAQT LARLLDVPFA MADATTLTEA GYVGEDVENI VQKLLQKADY DVEKAQKGII
     YIDEIDKITR KSENPSITRD VSGEGVQQAL LKMIEGTVAS IPPQGGRKHP QQEFIQIDTS
     NILFICGGAF AGLEKIVQQR QEKGGIGFTA DVKNKDETKK LAELFRQVEP TDLVKFGLIP
     EFIGRLPVIA TLEELDEEAL MQILTEPKNA LTRQYQYLFN MENVDLVFED SALRAVAKRA
     LERNTGARGL RSILENVLLE TMYDLPSRTD VGTVFINEAV INGEAEPVYK SERQPKEAVT
     HESVAKADLK VIDSKSA
//

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