ID B7AWD3_9FIRM Unreviewed; 465 AA.
AC B7AWD3;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE RecName: Full=ClpX-type ZB domain-containing protein {ECO:0000259|PROSITE:PS51902};
GN ORFNames=BACPEC_03033 {ECO:0000313|EMBL:EEC56524.1};
OS [Bacteroides] pectinophilus ATCC 43243.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=483218 {ECO:0000313|EMBL:EEC56524.1, ECO:0000313|Proteomes:UP000003136};
RN [1] {ECO:0000313|EMBL:EEC56524.1, ECO:0000313|Proteomes:UP000003136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43243 {ECO:0000313|EMBL:EEC56524.1,
RC ECO:0000313|Proteomes:UP000003136};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bacteroides pectinophilus (ATCC 43243).";
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEC56524.1, ECO:0000313|Proteomes:UP000003136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43243 {ECO:0000313|EMBL:EEC56524.1,
RC ECO:0000313|Proteomes:UP000003136};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000256|PROSITE-
CC ProRule:PRU01250}.
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:EEC56524.1}.
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DR EMBL; ABVQ01000037; EEC56524.1; -; Genomic_DNA.
DR AlphaFoldDB; B7AWD3; -.
DR STRING; 483218.BACPEC_03033; -.
DR eggNOG; COG1219; Bacteria.
DR HOGENOM; CLU_014218_8_2_9; -.
DR Proteomes; UP000003136; 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: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 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 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 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; 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};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|PROSITE-
KW ProRule:PRU01250};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01250}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU01250}.
FT DOMAIN 15..69
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000259|PROSITE:PS51902"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
SQ SEQUENCE 465 AA; 52034 MW; F8F62FF28F7BCAEC CRC64;
MSEDKINNTN DIVDSEKEDK DEYEKVCSVC RRPESKAGKL ITMPGNMYVC SDCMQRSFDM
INSNSNYDDL MKMMSNPSLG GMNIFMPGME DMEVPKKQRI KKRKKDEKAK PIIELKDIPA
PHEIKAKLDE YVIGQDYAKK VMSVAVYNHY KRVATDTMDD IEIEKSNMLM IGPTGSGKTY
LVKTLAKLLN VPLAIADATS LTEAGYIGDD IESVVSKLLA AADNDVDRAE QGIIFIDEID
KIAKKKETRS RDVSGESVQQ GMLKLLEGSD IEVPVGATSK NAMVPLTTVN TRNILFICGG
AFPELDEVIK ERLNEQASIG FIADLKDKYD NDDKLLSKVT LEDLRNFGMI PEFLGRLPVV
FTLDPLDKDM LVSILKEPKN AILKQYKKLL ALDEVELEFD DSALEAIAEK ALEKKTGARA
LRSIIEEFML DIMYEIPKDD NIGRVIITGD YINKKGGPVI QMRTV
//
