CLPX_NEIMB
ID CLPX_NEIMB Reviewed; 414 AA.
AC Q9JYY3;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=NMB1372;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
CC -!- FUNCTION: ATP-dependent specificity component of the Clp protease. It
CC directs the protease to specific substrates. Can perform chaperone
CC functions in the absence of ClpP. {ECO:0000255|HAMAP-Rule:MF_00175}.
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. {ECO:0000255|HAMAP-Rule:MF_00175}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000255|HAMAP-
CC Rule:MF_00175}.
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DR EMBL; AE002098; AAF41746.1; -; Genomic_DNA.
DR PIR; A81091; A81091.
DR RefSeq; NP_274390.1; NC_003112.2.
DR RefSeq; WP_002222327.1; NC_003112.2.
DR PDB; 6VFS; EM; 3.30 A; A/B/C/D/E/F=1-414.
DR PDB; 6VFX; EM; 2.90 A; A/B/C/D/E/F=1-414.
DR PDBsum; 6VFS; -.
DR PDBsum; 6VFX; -.
DR AlphaFoldDB; Q9JYY3; -.
DR SMR; Q9JYY3; -.
DR STRING; 122586.NMB1372; -.
DR PaxDb; Q9JYY3; -.
DR EnsemblBacteria; AAF41746; AAF41746; NMB1372.
DR KEGG; nme:NMB1372; -.
DR PATRIC; fig|122586.8.peg.1719; -.
DR HOGENOM; CLU_014218_8_2_4; -.
DR OMA; HYKRVQA; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0009376; C:HslUV protease complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
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 GO; GO:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
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 3D-structure; ATP-binding; Chaperone; Metal-binding; Nucleotide-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..414
FT /note="ATP-dependent Clp protease ATP-binding subunit ClpX"
FT /id="PRO_0000160391"
FT DOMAIN 1..49
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT REGION 44..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 120..127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00175"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:6VFX"
FT HELIX 82..99
FT /evidence="ECO:0007829|PDB:6VFX"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:6VFX"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:6VFX"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:6VFX"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:6VFX"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:6VFX"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:6VFX"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:6VFX"
FT HELIX 160..167
FT /evidence="ECO:0007829|PDB:6VFX"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:6VFX"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:6VFX"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:6VFX"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:6VFX"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:6VFX"
FT HELIX 205..215
FT /evidence="ECO:0007829|PDB:6VFX"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:6VFX"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:6VFX"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:6VFX"
FT HELIX 254..262
FT /evidence="ECO:0007829|PDB:6VFX"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:6VFX"
FT HELIX 282..286
FT /evidence="ECO:0007829|PDB:6VFX"
FT HELIX 291..297
FT /evidence="ECO:0007829|PDB:6VFX"
FT HELIX 301..305
FT /evidence="ECO:0007829|PDB:6VFX"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:6VFX"
FT HELIX 320..326
FT /evidence="ECO:0007829|PDB:6VFX"
FT HELIX 332..342
FT /evidence="ECO:0007829|PDB:6VFX"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:6VFX"
FT HELIX 351..362
FT /evidence="ECO:0007829|PDB:6VFX"
FT TURN 363..365
FT /evidence="ECO:0007829|PDB:6VFX"
FT HELIX 369..385
FT /evidence="ECO:0007829|PDB:6VFX"
FT TURN 386..388
FT /evidence="ECO:0007829|PDB:6VFX"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:6VFX"
FT HELIX 399..403
FT /evidence="ECO:0007829|PDB:6VFX"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:6VFX"
SQ SEQUENCE 414 AA; 45099 MW; BC48D54586E085F1 CRC64;
MSNENRTCSF CGKSKSHVKH LIEGENAFIC DECVSNCIEI LHEDGNDGTP SESAGGEPEE
SGKLPTPAEI VANLNDHVIG QEQAKKALAV SVYNHYKRLR HPKAGANVEL SKSNILLIGP
TGSGKTLLAQ SLARKLDVPF VMADATTLTE AGYVGEDVEQ IITKLLGKCD FDVEKAQRGI
VYIDEIDKIS RKSDNPSITR DVSGEGVQQA LLKLIEGTVA SVPPQGGRKH PNQEFINVDT
TNILFICGGA FAGLEKVIRQ RTEKGGIGFG ASVHSKDENA DITKLFGIVE PEDLIKFGLI
PELIGRLPVI ATLEELDEDA LINILTEPKN ALVKQYQALF GMENVELEFE EGALRSIARQ
AMERKTGARG LRSIVERCLL DTMYRLPDLK GLKKVVVGKA VIEEGREPEL VFES
