ID A0A561TAP9_9ACTN Unreviewed; 842 AA.
AC A0A561TAP9;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:TWF84176.1};
GN ORFNames=FHX78_111110 {ECO:0000313|EMBL:TWF84176.1};
OS Streptomyces capillispiralis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68182 {ECO:0000313|EMBL:TWF84176.1, ECO:0000313|Proteomes:UP000316603};
RN [1] {ECO:0000313|EMBL:TWF84176.1, ECO:0000313|Proteomes:UP000316603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41695 {ECO:0000313|EMBL:TWF84176.1,
RC ECO:0000313|Proteomes:UP000316603};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
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:TWF84176.1}.
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DR EMBL; VIWV01000001; TWF84176.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A561TAP9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000316603; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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; 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 InterPro; IPR001943; UVR_dom.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
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; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
DR PROSITE; PS50151; UVR; 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:TWF84176.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TWF84176.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 31..179
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 446..481
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 75..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 442..488
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 842 AA; 92264 MW; CEF6D6D3022719CC CRC64;
MTNGFVGPEG DPFAEFLARF FGGQRPRQID IGRLLSQPAR ELVRGAAQYA AEHGSRDLDT
QHLLRAALAA EPTRSLLSRA GADPDSLASQ IDDRSGPVQH GPGDAPPPTS LSLTPAVKRA
LLDAHEMARA SGAGYIGPEH VLSALAANPD SAAGHILHAA RFAPSGPPEA AEAPPSRTER
PRPATGTPTL DKYGRDLTAL AREGRVDPVI GRDQEIEQTV EVLSRRGKNN PVLIGDAGVG
KTAVVEGLAQ RIAEGDVPDI LLGRRVVALD LTGVVAGTRY RGDFEERMNH IVEEIRSHSD
RLIVFIDELH TVVGAGGGGE GGSMDAGNIL KPALARGELH IVGATTLEEY RRIEKDAALA
RRFQPIMVPE PTPADAIEIL RGLRDRYEAH HQVRYTDEAL MAAVELSDRH LSDRRLPDKA
IDLIDQAGAR VRLRARTKGT DVRAMEREVE QLTCDKDQAV ADEQYEQATQ LRDRIVELKR
RIAEAGGDDE VDEGQSLWVD SEAIAEVVAR QTGIPVSRLT EEEKDRLLGL EQHLHQRVVG
QDEAVRVVSD AVLRSRAGLG SPDRPIGSFL FLGPTGVGKT ELARALAEAL FGSVDRMVRL
DMSEYQERHT VSRLVGAPPG YVGHEEAGQL TEVVRRHPYS LLLLDEVEKA HPDVFNILLQ
VLDDGRLTDS QGRTVDFTHT VIVMTSNLGS EAITRRGATL GFATGDAEAD EEARREQVLR
PLREHFRPEF LNRIDEVVVF RQLTAEELRR ITDLLLENTR RALKGQGIAV DFTDAAVDWL
AERGHQPEYG ARPLRRTIQR EVDNELSRLL LDGRVREGGR VTVDAEDGRL TFRTQETPAA
EL
//