CLPX_CAUVN
ID CLPX_CAUVN Reviewed; 420 AA.
AC B8GX14; O87708;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 83.
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}; OrderedLocusNames=CCNA_02039;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10322004; DOI=10.1128/jb.181.10.3039-3050.1999;
RA Osteras M., Stotz A., Schmid Nuoffer S., Jenal U.;
RT "Identification and transcriptional control of the genes encoding the
RT Caulobacter crescentus ClpXP protease.";
RL J. Bacteriol. 181:3039-3050(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=NA1000 / CB15N;
RX PubMed=9755166; DOI=10.1093/emboj/17.19.5658;
RA Jenal U., Fuchs T.;
RT "An essential protease involved in bacterial cell-cycle control.";
RL EMBO J. 17:5658-5669(1998).
RN [4]
RP FUNCTION, SUBSTRATE, INTERACTION WITH SOCA, DOMAIN, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF LEU-13 AND ILE-47.
RX PubMed=24239291; DOI=10.1016/j.molcel.2013.10.014;
RA Aakre C.D., Phung T.N., Huang D., Laub M.T.;
RT "A bacterial toxin inhibits DNA replication elongation through a direct
RT interaction with the beta sliding clamp.";
RL Mol. Cell 52:617-628(2013).
CC -!- FUNCTION: ATP-dependent specificity component of the Clp protease (By
CC similarity). It directs the protease to specific substrates (By
CC similarity). Required for degradation of response regulator CtrA, thus
CC contributing to the G1-to-S transition (PubMed:9755166). Required to
CC degrade DNA replication inhibitor toxin SocB, this function is probably
CC the reason why the protease is essential in this organism
CC (PubMed:24239291). Can perform chaperone functions in the absence of
CC ClpP (By similarity). {ECO:0000255|HAMAP-Rule:MF_00175,
CC ECO:0000269|PubMed:24239291, ECO:0000269|PubMed:9755166}.
CC -!- SUBUNIT: Component of the ClpX-ClpP complex. Forms a hexameric ring
CC that, in the presence of ATP, binds to fourteen ClpP subunits assembled
CC into a disk-like structure with a central cavity, resembling the
CC structure of eukaryotic proteasomes (By similarity). Interacts with
CC SocA (PubMed:20472802). {ECO:0000255|HAMAP-Rule:MF_00175,
CC ECO:0000269|PubMed:24239291}.
CC -!- DOMAIN: The N-terminal domain (residues 1-62) is required for
CC interaction with SocA and targeting of SocB for degradation by ClpXP.
CC {ECO:0000269|PubMed:24239291}.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted (PubMed:9755166,
CC PubMed:24239291). When depleted for ClpX cells arrest before the
CC initiation of chromosome replication and are blocked in the cell
CC division process (PubMed:9755166). In depletion experiments ClpX
CC protein starts to decline after about 4 hours, which coincides with
CC cell filamention and a 1000-fold loss of viability by 12 hours; SocB
CC protein accumulates. Deletion of socB permits slower than wild-type
CC growth of the clpX disruption. {ECO:0000269|PubMed:24239291,
CC ECO:0000269|PubMed:9755166}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000255|HAMAP-
CC Rule:MF_00175}.
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DR EMBL; AJ010321; CAA09092.1; -; Genomic_DNA.
DR EMBL; CP001340; ACL95504.1; -; Genomic_DNA.
DR RefSeq; WP_010919827.1; NC_011916.1.
DR RefSeq; YP_002517412.1; NC_011916.1.
DR AlphaFoldDB; B8GX14; -.
DR SMR; B8GX14; -.
DR PRIDE; B8GX14; -.
DR EnsemblBacteria; ACL95504; ACL95504; CCNA_02039.
DR GeneID; 7333370; -.
DR KEGG; ccs:CCNA_02039; -.
DR PATRIC; fig|565050.3.peg.1996; -.
DR HOGENOM; CLU_014218_8_2_5; -.
DR OMA; HYKRVQA; -.
DR OrthoDB; 718259at2; -.
DR PhylomeDB; B8GX14; -.
DR PRO; PR:B8GX14; -.
DR Proteomes; UP000001364; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
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 Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 6.20.220.10; -; 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; IPR046425; ClpX_bact.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010603; Znf_CppX_C4.
DR InterPro; IPR038366; Znf_CppX_C4_sf.
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.
DR PROSITE; PS51902; CLPX_ZB; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Metal-binding; Nucleotide-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..420
FT /note="ATP-dependent Clp protease ATP-binding subunit ClpX"
FT /id="PRO_0000378282"
FT DOMAIN 3..56
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT REGION 1..62
FT /note="Required for interaction of SocA with this protein
FT and degradation of SocB by ClpXP"
FT /evidence="ECO:0000269|PubMed:20472802"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 119..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00175"
FT MUTAGEN 13
FT /note="L->A: Disrupts interaction with SocA but not self-
FT association."
FT /evidence="ECO:0000269|PubMed:24239291"
FT MUTAGEN 47
FT /note="I->A: Disrupts interaction with SocA but not self-
FT association."
FT /evidence="ECO:0000269|PubMed:24239291"
SQ SEQUENCE 420 AA; 45860 MW; 036339E2AB315C11 CRC64;
MTKAASGDTK STLYCSFCGK SQHEVRKLIA GPTVFICDEC VELCMDIIRE EHKIAFVKSK
DGVPTPREIC EVLDDYVIGQ GHAKKVLAVA VHNHYKRLNH ASKNNDVELA KSNILLVGPT
GTGKTLLAQT LARIIDVPFT MADATTLTEA GYVGEDVENI VLKLLQAADY NVERAQRGIV
YIDEIDKISR KSDNPSITRD VSGEGVQQAL LKIMEGTVAS VPPQGGRKHP QQEFLQVDTT
NILFICGGAF AGLEKIISAR GAAKSIGFGA KVTDPEERRT GEILRNVEPD DLQRFGLIPE
FIGRLPVVAT LEDLDEAALV KILTEPKNAF VKQYQRLFEM ENIGLTFTED ALHQVAKKAI
ARKTGARGLR SIMEGILLET MFELPTYEGV EEVVVNAEVV EGRAQPLLIY AEKKGGAASA
