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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//