ID C4ZHC1_AGARV Unreviewed; 509 AA.
AC C4ZHC1;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 90.
DE SubName: Full=ATP-dependent protease ATPase subunit clpX {ECO:0000313|EMBL:ACR74933.1};
GN OrderedLocusNames=EUBREC_1171 {ECO:0000313|EMBL:ACR74933.1};
OS Agathobacter rectalis (strain ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835
OS / VPI 0990) (Eubacterium rectale).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Agathobacter.
OX NCBI_TaxID=515619 {ECO:0000313|EMBL:ACR74933.1, ECO:0000313|Proteomes:UP000001477};
RN [1] {ECO:0000313|EMBL:ACR74933.1, ECO:0000313|Proteomes:UP000001477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835 / LMG 30912 / VPI
RC 0990 {ECO:0000313|Proteomes:UP000001477};
RX PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA Hettich R.L., Gordon J.I.;
RT "Characterizing a model human gut microbiota composed of members of its two
RT dominant bacterial phyla.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
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DR EMBL; CP001107; ACR74933.1; -; Genomic_DNA.
DR RefSeq; WP_012742034.1; NC_012781.1.
DR AlphaFoldDB; C4ZHC1; -.
DR STRING; 515619.EUBREC_1171; -.
DR PaxDb; 515619-EUBREC_1171; -.
DR KEGG; ere:EUBREC_1171; -.
DR HOGENOM; CLU_014218_8_2_9; -.
DR OMA; KSNMLMI; -.
DR Proteomes; UP000001477; Chromosome.
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:0051082; F:unfolded protein 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 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 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 Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Hydrolase {ECO:0000313|EMBL:ACR74933.1};
KW Protease {ECO:0000313|EMBL:ACR74933.1}.
FT DOMAIN 199..359
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 401..496
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 509 AA; 56590 MW; 97ACD976402B2551 CRC64;
MNNDDFKEVP DNIQDNNGET TNNIDNTNDN KSNDYEDVCY ICRRPESVAG KMIHIQPNLC
ICNDCMQKTF DSMSNGNFGN LGNLGNISNM DFGNMPNISM INLSDLTGGI PNSQKLKKKK
PKEEKKVEPI LDIHSIPAPH RIKASLDDYV VGQEHAKKVM SVAVYNHYKR VMADNKHKAQ
EENTTAKQAS NKYDGVEIEK SNMLMIGPTG SGKTYLVKTL AKLLDVPLAI TDATSLTEAG
YIGDDIESVV SKLLAAADND VERAEHGIIF IDEIDKLAKK RNANQRDVSG ESVQQGMLKL
LEGSEVEVPV GASSKNAMVP MTTVDTRNIL FICGGAFPGL EDIIKERLNK EASIGFKADL
KDKYDGDENL LMQATVDDIR KFGMIPEFIG RLPIMFSLEA LTEDMLVKIL KEPKNAIIKQ
YQKLLEMDEV RLEFDDDALY AIAKMAKEKK VGARALRAII EDFMLDIMYE IPKDDNIGTV
TITKDYVEKK GGPLIQMRGT PELADSQHV
//