ID A0A1M6VAW0_9FIRM Unreviewed; 475 AA.
AC A0A1M6VAW0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000313|EMBL:SHK78633.1};
GN ORFNames=SAMN02745136_03350 {ECO:0000313|EMBL:SHK78633.1};
OS Anaerocolumna jejuensis DSM 15929.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerocolumna.
OX NCBI_TaxID=1121322 {ECO:0000313|EMBL:SHK78633.1, ECO:0000313|Proteomes:UP000184386};
RN [1] {ECO:0000313|EMBL:SHK78633.1, ECO:0000313|Proteomes:UP000184386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15929 {ECO:0000313|EMBL:SHK78633.1,
RC ECO:0000313|Proteomes:UP000184386};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FRAC01000017; SHK78633.1; -; Genomic_DNA.
DR RefSeq; WP_073277997.1; NZ_FRAC01000017.1.
DR AlphaFoldDB; A0A1M6VAW0; -.
DR STRING; 1121322.SAMN02745136_03350; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000184386; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:SHK78633.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Hydrolase {ECO:0000313|EMBL:SHK78633.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:SHK78633.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184386};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 163..322
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 365..457
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 475 AA; 52977 MW; BEE33385D059E414 CRC64;
MSDDLKDQDN NLENIDKETK NKDDYEEVCY ICRRPESKVG KMLRIPNNIS ICSDCMQKTF
DTINSNGMPY MDLMGFPPNV MNMNTVQKEV PKNQKLKKKK AEEEPAETAD AFDIKNIPSP
HVIKGKLDDY VVGQEHGKKV LSVAVYNHYK RVAADTMDDI EIEKSNMLMI GPTGSGKTFL
VKTLARLLDV PLAITDATSL TEAGYIGDDV ESVISKLLAA ADNDVERAEK GIIFIDEIDK
IAKKKNTNNR DVSGESVQQG LLKLLEGSDV EVPVGATSKN AMVPLTTVNT KNILFICGGA
FPDLDTIIKT RLNKQTSIGF SADLKDKYDS DPNVLLKVSV EDLREFGMIP EFLGRLPIMF
SLEGLTKDML IKILKEPKNA ILKQYQKLLA LDEVCLEFDD GAMEAIAEKA MEKKTGARAL
RAIIEDFMLD IMYEIPKDIN IGKVTITRDY IEKKGVPQIE MRGSNYKNLL LEGSN
//
