ID A0A1M7L3W3_9FIRM Unreviewed; 487 AA.
AC A0A1M7L3W3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000313|EMBL:SHM72445.1};
GN ORFNames=SAMN02746066_03045 {ECO:0000313|EMBL:SHM72445.1};
OS Anaerosporobacter mobilis DSM 15930.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerosporobacter.
OX NCBI_TaxID=1120996 {ECO:0000313|EMBL:SHM72445.1, ECO:0000313|Proteomes:UP000184038};
RN [1] {ECO:0000313|EMBL:SHM72445.1, ECO:0000313|Proteomes:UP000184038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15930 {ECO:0000313|EMBL:SHM72445.1,
RC ECO:0000313|Proteomes:UP000184038};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FRCP01000015; SHM72445.1; -; Genomic_DNA.
DR RefSeq; WP_073289251.1; NZ_FRCP01000015.1.
DR AlphaFoldDB; A0A1M7L3W3; -.
DR STRING; 1120996.SAMN02746066_03045; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000184038; 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 CDD; cd19497; RecA-like_ClpX; 1.
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:SHM72445.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Hydrolase {ECO:0000313|EMBL:SHM72445.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:SHM72445.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184038};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 179..338
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 381..475
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 54632 MW; A68241D72075B86C CRC64;
MSDDMNKDIE YNLTESNKED KQEVKDSAKD KKIIDKEKEY KDDYEDICYI CRRPESKVGK
MIHIPNNICI CSDCMQKTFD TINTGNVPYM DMMNLGPMMN FSGIQNEIPK SQKLKKKKEE
KKEDTKTIDL KNIPAPHVIK RQLDDYVIGQ EHAKKVISVA VYNHYKRVAA NAMDDIEIEK
SNMLMIGPTG CGKTYLVKTL ARLLNVPLAI TDATALTEAG YIGDDVESVI SKLLAAADND
VEKAERGIVF IDEIDKIAKK KSTTNRDVSG ESVQQGMLKL LEGAEVEVPV GATNKNAMVP
LTTVNTKNIL FICGGAFPDL EKIIKARLNK KSSIGFGAEL KDKYDTETNL LQKVTVDDLR
EFGMIPEFIG RLPVIYSLEG LTKEMLVEVL KEPKNAILKQ YKKLLALDEV DLIFDDGALE
AIAEKALEKK TGARALRAII EEFMLDIMYE IPKDDNIGRV TITRDYIEKK GGPVIEMRGC
ITPLLTE
//