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Database: UniProt
Entry: W4V802_9FIRM
LinkDB: W4V802_9FIRM
Original site: W4V802_9FIRM 
ID   W4V802_9FIRM            Unreviewed;       800 AA.
AC   W4V802;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:GAE88879.1};
GN   ORFNames=JCM21531_2361 {ECO:0000313|EMBL:GAE88879.1};
OS   Acetivibrio straminisolvens JCM 21531.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Acetivibrio.
OX   NCBI_TaxID=1294263 {ECO:0000313|EMBL:GAE88879.1, ECO:0000313|Proteomes:UP000019109};
RN   [1] {ECO:0000313|EMBL:GAE88879.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 21531 {ECO:0000313|EMBL:GAE88879.1};
RA   Yuki M., Oshima K., Suda W., Sakamoto M., Kitamura K., Iida T., Hattori M.,
RA   Ohkuma M.;
RT   "Draft Genome Sequence of Clostridium straminisolvens Strain JCM 21531T,
RT   Isolated from a Cellulose-Degrading Bacterial Community.";
RL   Genome Announc. 2:e00110-14(2014).
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:GAE88879.1}.
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DR   EMBL; BAVR01000026; GAE88879.1; -; Genomic_DNA.
DR   RefSeq; WP_038289044.1; NZ_BAVR01000026.1.
DR   AlphaFoldDB; W4V802; -.
DR   STRING; 1294263.JCM21531_2361; -.
DR   Proteomes; UP000019109; 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 4.10.860.10; UVR domain; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR001270; ClpA/B.
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:SF193; CHAPERONE PROTEIN CLPB; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:GAE88879.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:GAE88879.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:GAE88879.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019109}.
FT   DOMAIN          181..326
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          513..677
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          684..773
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          104..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          776..800
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          386..413
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   800 AA;  89988 MW;  A35D6F397E273072 CRC64;
     MMMCSICKEN LAVVFITKIV NGKQTQEGLC FSCAKKQGIQ PINQILEQTG ISDEEIDDLN
     KQVGSFFEDM DFSSMNDTEA GPNSANPFLN LINKSLNRTM DSMGIKGTKE ETESDSKAER
     EDKDKSNTRT KTQDKKAPKK KKYLDTYGTN LITKAKEGKI DRVIGRNREI ERVIQILNRR
     NKNNPVLIGE PGVGKTAIAE GLAVRIINRD VPAKLFNAEV YVLDLTSIVA GTQFRGQFEN
     RMKGIIEECK SLGNIILVID EIHNIMGAGE AEGAMNAANI LKPALAKGEI QVIGATTLDE
     YRKHIEKDSA LERRFQPVLV DEPTVEETIE ILQGIKDYYE SYHRVKISDE VIRAAAVLSE
     RYITDRFLPD KAIDVLDEAG SRANIKNVAL LEYEALKEEL RKVQEEKENA VSADSIEDYQ
     KAADLKVREC KLLQQIKEIE HKNKDMELTV DDIAYVIESW TKIPVQRLTE VEAKKLLNLE
     ERLHNRVIGQ HQAVSSVAKA IRRSRADFKK RKKPASFIFV GPTGVGKTEL VRALAVELFE
     SEEALIRLDM SEYMEKHTVS KLIGAPPGYV GYDEGGQLTE KVRRKPYSVI LLDEIEKAHP
     DVFNMLLQIL EDGRATDSHG RTVSFENTVL IMTSNAGTSL KASSIGFAND NYIAMENKIK
     EVLKETFRPE FLNRIDEIIV FNELTRDELK QIVDLMLKDV VEEVESKKMS IKFEDGVREF
     VLEKGYDPKY GARPLRRTIQ KYIEDELTEM YLKGMFAEGS NIVVGVRDGN IAFNVESPAE
     EPTEGPAVDT EGPTLDSSNA
//
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