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Database: UniProt
Entry: A4AG53_9ACTN
LinkDB: A4AG53_9ACTN
Original site: A4AG53_9ACTN 
ID   A4AG53_9ACTN            Unreviewed;       717 AA.
AC   A4AG53;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=ATP-dependent Clp protease, ATP-binding subunit {ECO:0000313|EMBL:EAR25959.1};
GN   ORFNames=A20C1_08763 {ECO:0000313|EMBL:EAR25959.1};
OS   marine actinobacterium PHSC20C1.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=312284 {ECO:0000313|EMBL:EAR25959.1, ECO:0000313|Proteomes:UP000003868};
RN   [1] {ECO:0000313|EMBL:EAR25959.1, ECO:0000313|Proteomes:UP000003868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHSC20C1 {ECO:0000313|EMBL:EAR25959.1,
RC   ECO:0000313|Proteomes:UP000003868};
RA   Murray A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|ARBA:ARBA00026057}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, 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:EAR25959.1}.
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DR   EMBL; AAOB01000002; EAR25959.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4AG53; -.
DR   STRING; 312284.A20C1_08763; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_11; -.
DR   Proteomes; UP000003868; 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; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
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:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 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; 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   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:EAR25959.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:EAR25959.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003868}.
FT   DOMAIN          52..197
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          451..619
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          618..709
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   COILED          266..346
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   717 AA;  79198 MW;  2DC555BE15170DCF CRC64;
     MQGAPSTDDE QKSALEKYGV NLTEIARSGK LDPVIGRDAE IRRVSQVLTR RTKNNPVLIG
     EPGVGKTAVV EGLAQRIIAG DVADSLKNKQ LVSLDLAALV AGAKYRGEFE ERLKAVLKEI
     KESDGEVITF IDELHTLMGA GGGDGSVAAS NMLKPMLARG ELRLIGATTL DEYRQYIEKD
     AALERRFQQV FVGEPSVEDT VAILRGLKER YEAHHKVAIA DSALVSAATL SNRYISGRKL
     PDKAIDLIDE AASRLKMEID SSPVEIDQLK RAVDRLRIEE LALKKEKDDA SKARLAKLRE
     DLAVQGKHLS ELEARWKIEK SSLTGVGDLK TRLNDARIEL DRAMRDGEYQ KASKLNYETI
     PSIEEALVTA ESNEPSGPRM VNDQVTEEDI AAVVAAWTGI PVDRLTEGET EKLLHLEAEL
     GKRLIGQKEA VQAVSEAVRR TRAGISDPDR PTGSFLFLGP TGVGKTELAK ALAQYLFNDE
     KALVRIDMSE YGEKFSVSRL VGAPPGYIGY EQGGQLTEAV RRRPYSVILL DEVEKAHPEV
     FDVLLQVLDD GRLTDGQGRT VDFRNVILIL TSNLGSQFIT EQALPWEARK SAVHDLVRKS
     FKPEFINRLD DIVVFQPLST DDLSQIVELD IDRLSKRLTD RRLELAVTPD ARTWLAERGY
     DPIYGARPLR RLMQREIDDR LAKALLAGDI RDGDTVFVAL ASDGDALVVS RMQPGNS
//
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