ID   C0MEW8_STRS7            Unreviewed;       697 AA.
AC   C0MEW8;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Putative ATP-dependent protease ATP-binding subunit ClpL {ECO:0000313|EMBL:CAW99127.1};
GN   OrderedLocusNames=SZO_08950 {ECO:0000313|EMBL:CAW99127.1};
OS   Streptococcus equi subsp. zooepidemicus (strain H70).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553483 {ECO:0000313|Proteomes:UP000001368};
RN   [1] {ECO:0000313|EMBL:CAW99127.1, ECO:0000313|Proteomes:UP000001368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H70 {ECO:0000313|EMBL:CAW99127.1,
RC   ECO:0000313|Proteomes:UP000001368};
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA   Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA   Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA   Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA   Maskell D.J., Parkhill J., Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(2009).
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DR   EMBL; FM204884; CAW99127.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0MEW8; -.
DR   KEGG; seq:SZO_08950; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_3_9; -.
DR   Proteomes; UP000001368; Chromosome.
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:CAW99127.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Hydrolase {ECO:0000313|EMBL:CAW99127.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:CAW99127.1}.
FT   DOMAIN          111..258
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          442..593
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          607..694
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
SQ   SEQUENCE   697 AA;  76821 MW;  844A03D44FB78200 CRC64;
     MTTYYGKDPF GNMDDIFNQL MGNIGGYRSE NRRYLVNGRE MTPEEFQEYR KTGKLAATEG
     QDKQAGSLKK DGILTKLGTN LTEEARQGRL DPVIGRNDEI QATAEILARR IKNNPVLVGD
     AGVGKTAVVE GLAQAIVNGD VPAAIKNKEI ISIDISGLEA GTQYRGSFEE NIQNMVKEVK
     EAGNIILFFD EIHQILGAGS AGSDSGSKGL ADILKPALSR GELTLIGATT QDEYRNTILK
     NAALARRFNE VKVNAPSAED TFHILMGIRN LYEQHHNVIL PDSVLKAAID YAIQYIPQRS
     LPDKAIDLVD MTAAHLAAQH PVTDLKSLEA EIAKQKELQE KAVAAEDFEK ALTAKTRIEE
     LQKQINHHSE GQKVTATVND IAESVERLTG VPVSNMGAND LERLKEISNR LKGHVIGQDG
     AVEAVARAIR RNRAGFDDGN RPIGSFLFVG PTGVGKTELA KQLALDMFGS KDAIIRLDMS
     EYSDRTAVSK LIGTTAGYVG YDDNQNTLTE RVRRSPYSII LLDEIEKADP QVITLLLQVL
     DDGRLTDGQG NTINFKNTVI IATSNAGFGH QAGERADQEP AIMERIAPYF RPEFLNRFNG
     VIEFNHLAKK DLQEIVALML TEVNQTLAKK GISLEVTDDV KERLIDLGYD HAMGVRPLRR
     VIEQEIRDRI TDYYLDHPTA KHLLASLDQD TITISEK
//