ID B3C5G8_9BACE Unreviewed; 742 AA.
AC B3C5G8;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 24-JAN-2024, entry version 81.
DE SubName: Full=Putative ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:EDV07752.1};
GN ORFNames=BACINT_00150 {ECO:0000313|EMBL:EDV07752.1};
OS Bacteroides intestinalis DSM 17393.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=471870 {ECO:0000313|EMBL:EDV07752.1, ECO:0000313|Proteomes:UP000004596};
RN [1] {ECO:0000313|EMBL:EDV07752.1, ECO:0000313|Proteomes:UP000004596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV07752.1,
RC ECO:0000313|Proteomes:UP000004596};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bacteroides intestinalis (DSM 17393).";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDV07752.1, ECO:0000313|Proteomes:UP000004596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV07752.1,
RC ECO:0000313|Proteomes:UP000004596};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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:EDV07752.1}.
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DR EMBL; ABJL02000001; EDV07752.1; -; Genomic_DNA.
DR RefSeq; WP_007659765.1; NZ_ABJL02000001.1.
DR AlphaFoldDB; B3C5G8; -.
DR STRING; 471870.BACINT_00150; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000004596; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF111; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPA; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Hydrolase {ECO:0000313|EMBL:EDV07752.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:EDV07752.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 200..346
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 481..628
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 648..737
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 742 AA; 83516 MW; A7787B3D3AC88443 CRC64;
MDIQNTVHVN SAFTYAQKKA ISYRHEFITP EHLLSAFLEQ SPFANALNMC FCDTQELAFS
LENYFTEELE SVPADMDYEL EVSTQLNELI QHAYLMIDYS SAEALNVPHL VQSMLQLKDS
WACHILKEAL EEDLPEFISQ LISRYEEVEE EDNLQTSPQE KSEPWRNFVT CLNDCLQDHN
PLIGREAELE RTIQVLCRKE KNNPLHVGEP GVGKTSLAYG LAARIEAREV PERLLDCRIY
ELDLGTLLAG TQYRGDFEKR LKTIMEGVRN EGRAIIYIDE IHNLIGAGRT GDGSMDASNM
LKPYLESGDI RFIGSTTYEE YNRYFARSKG LVRRFQQIDI HEPSIEETIH IVEGLKEKYE
EFHGVTYQPD VIPYAVKASV RYISDRFLPD KAIDLVDEAG AYREIHPIPS GEQIVDKTLI
TDVLARICKV DALAMKEEDT TSLETLHARI SAKIYGQEEA VRQVVEAVQM SKAGLLDENK
PLASLLFVGP TGVGKTEVAK VLASELGISL QRFDMSEYTE KHTVAKLIGS PAGYVGYEDG
GLLTDAIRKT PNCVLLLDEI EKAHPDVFNI LLQVMDYAVL TDNKGRKADC RHVVLIMTSN
AGAQFARQAS IGFSSQITAG EAMLKQVKKT FKPEFINRLS ATVVFHDMSR KMASLILDKK
LGELSSKLAS RQIEMGLSPE ARNWLLQRGF LPEYGAREMD RVIASHLKPL LMREILFGSL
KSGGKTCIQV DKDQLVLQLS TK
//