ID C6WWC7_METML Unreviewed; 426 AA.
AC C6WWC7;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000256|HAMAP-Rule:MF_00175};
GN Name=clpX {ECO:0000256|HAMAP-Rule:MF_00175};
GN OrderedLocusNames=Mmol_1320 {ECO:0000313|EMBL:ACT48226.1};
OS Methylotenera mobilis (strain JLW8 / ATCC BAA-1282 / DSM 17540).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylotenera.
OX NCBI_TaxID=583345 {ECO:0000313|EMBL:ACT48226.1, ECO:0000313|Proteomes:UP000002742};
RN [1] {ECO:0000313|Proteomes:UP000002742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLW8 / ATCC BAA-1282 / DSM 17540
RC {ECO:0000313|Proteomes:UP000002742};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Kayluzhnaya M., Chistoserdova L.;
RT "Complete sequence of Methylotenera mobilis JLW8.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACT48226.1, ECO:0000313|Proteomes:UP000002742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLW8 / ATCC BAA-1282 / DSM 17540
RC {ECO:0000313|Proteomes:UP000002742};
RX PubMed=21622745; DOI=10.1128/JB.00404-11;
RA Lapidus A., Clum A., Labutti K., Kaluzhnaya M.G., Lim S., Beck D.A.,
RA Glavina Del Rio T., Nolan M., Mavromatis K., Huntemann M., Lucas S.,
RA Lidstrom M.E., Ivanova N., Chistoserdova L.;
RT "Genomes of three methylotrophs from a single niche uncover genetic and
RT metabolic divergence of Methylophilaceae.";
RL J. Bacteriol. 193:3757-3764(2011).
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:0000256|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:0000256|HAMAP-Rule:MF_00175}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000256|HAMAP-
CC Rule:MF_00175, ECO:0000256|PROSITE-ProRule:PRU01250}.
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DR EMBL; CP001672; ACT48226.1; -; Genomic_DNA.
DR RefSeq; WP_015832261.1; NC_012968.1.
DR AlphaFoldDB; C6WWC7; -.
DR STRING; 583345.Mmol_1320; -.
DR KEGG; mmb:Mmol_1320; -.
DR eggNOG; COG1219; Bacteria.
DR HOGENOM; CLU_014218_8_2_4; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000002742; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19497; RecA-like_ClpX; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 6.20.220.10; ClpX chaperone, C4-type zinc finger domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00382; clpX; 1.
DR PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51902; CLPX_ZB; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00175};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00175};
KW Hydrolase {ECO:0000313|EMBL:ACT48226.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00175};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00175}; Protease {ECO:0000313|EMBL:ACT48226.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002742};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00175}.
FT DOMAIN 1..54
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000259|PROSITE:PS51902"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 124..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ SEQUENCE 426 AA; 46660 MW; C361A0FCEA4D686C CRC64;
MATKADDDKL LYCSFCGKSQ HEVKKLIAGP SVFICNECVD LCNDIIKEEI QNSDGLKSTD
TSLPTPQEIC KILDQYVIGQ TQAKKNLAVA VYNHYKRLGH NNLANGGQKD EVEIAKSNIL
LIGPTGSGKT LLAQTLARLL DVPFVMADAT TLTEAGYVGE DVENIMQKLL QKCDYDTEKA
QRGIVYIDEV DKISRKSDNP SITRDVSGEG VQQALLKLIE GTVASIPPQG GRKHPNQEFV
QLDTTNILFI CGGAFDGLEK VIRLRSEKGG IGFGAEVKSK ADVREVGAVL RDVEPEDLIK
FGLIPEFIGR LPVVATLESL DEAALMTILT EPKNALTKQY IKLFKMEGVD LEFRESALLL
IAKKALERKT GARGLRSIME HSLLEVMYEL PSLKNLSKVV IDDGVIRGDS PPLLIYEDKP
ADEASA
//
