ID F3AH36_9FIRM Unreviewed; 475 AA.
AC F3AH36;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE SubName: Full=ATP-dependent Clp protease {ECO:0000313|EMBL:EGG81198.1};
GN ORFNames=HMPREF0992_02381 {ECO:0000313|EMBL:EGG81198.1};
OS Lachnospiraceae bacterium 6_1_63FAA.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=658083 {ECO:0000313|EMBL:EGG81198.1, ECO:0000313|Proteomes:UP000004368};
RN [1] {ECO:0000313|EMBL:EGG81198.1, ECO:0000313|Proteomes:UP000004368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6_1_63FAA {ECO:0000313|EMBL:EGG81198.1,
RC ECO:0000313|Proteomes:UP000004368};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Ambrose C., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., White J.,
RA Yandava C., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 6_1_63FAA.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGG81198.1}.
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DR EMBL; ACTV01000024; EGG81198.1; -; Genomic_DNA.
DR AlphaFoldDB; F3AH36; -.
DR HOGENOM; CLU_014218_8_2_9; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000004368; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Hydrolase {ECO:0000313|EMBL:EGG81198.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:EGG81198.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 166..327
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 368..463
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 53521 MW; 882A446052DDC4D3 CRC64;
MSDDKEYLKT NNPSEETDEK ENKDQYEKIC FMCRRPESKA GKMIDLPNDI HICTDCMQRS
FDTMNNSNIN YDELMRNMPN ISMIDLSSLQ NQIPNRQKVK KKQEAPKEKV APKVFDIKSI
PAPHKIKASL DEYVIGQEKA KKVMSVAVYN HYKRVFADMN DDIEIEKSNM LMIGPTGSGK
TYLVKTLARL LDVPLAITDA TSLTEAGYIG DDIESVVSKL LAAADNDVER AEHGIIFIDE
IDKIAKKKNT NQRDVSGEAV QQGMLKLLEG SEIEVPVGAN SKNAMVPLTT VNTKNILFIC
GGAFPDLEEI IKERLNKTAS IGFQADLKDK YDHDNTLLEK VTVDDIKKFG MIPEFLGRLP
IIFTLTGLNR DMLVEILKEP KNAILKQYQK LLALDEVKLE FEDGALEAIA DMALEKHTGA
RALRAILEEY MLDIMYEIPK DDSIGEVIIT KEYIEHTGGP RILLRGQEMP MLEAK
//