ID A0A1H4L879_9ACTN Unreviewed; 843 AA.
AC A0A1H4L879;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:SEB66944.1};
GN ORFNames=SAMN05216482_0465 {ECO:0000313|EMBL:SEB66944.1};
OS Streptomyces sp. PAN_FS17.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1855351 {ECO:0000313|EMBL:SEB66944.1, ECO:0000313|Proteomes:UP000199275};
RN [1] {ECO:0000313|Proteomes:UP000199275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAN_FS17 {ECO:0000313|Proteomes:UP000199275};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNTN01000001; SEB66944.1; -; Genomic_DNA.
DR RefSeq; WP_030947455.1; NZ_FNTN01000001.1.
DR AlphaFoldDB; A0A1H4L879; -.
DR STRING; 1855351.SAMN05216482_0465; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199275; 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:SEB66944.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SEB66944.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199275};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 38..180
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 450..485
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 822..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 465..492
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 822..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 843 AA; 91647 MW; CDEA3A8B74053441 CRC64;
MSMSSFGFGS PDPFSDMLNR FFGMSPASSP PAVQRVPIGR LLTESSQELL NLAAGRAMED
GTSDLDTEHL LWAATQVEPA RSLLARAEVN PDVLGAEIAK ILPHESVEPS SEPGLTPAAK
RTLAAAYARS QAAGVSYIGP EHILGALISD ADSGAARLLQ AEGQDVGRLA GVTEQAARTE
GQPADRNQQP ATTLDEFGRD LTDEAKAGKL DPVVGRAEEI EETVEILSRR SKNNPVLIGE
PGVGKTAIVE GLAQRIVAGE VPDTLKDKRV VALDLSGMVA GAQYRGQFEE RLKKVIEDVQ
AASGDIILFI DELHTVVGAG ATGEGSMDAG NMLKPALARG ELHVVGATTI DEYRKYVEKD
AALERRFQPV MIPEPTVEET VQILEGLRDA YEAHHQVRFA DGALAAAAEL SDRYISDRFL
PDKAIDVMDQ AGARVRLRSA GRSTEVVSRE DRIAKLRREQ DQAVAAEDFE KAARMKREIA
QAEGELAGIE ERREGVVSVT DADIADVVSR RTGIPVSQLT ATEKEKLLGL EERMHSRIVG
QDEAVSAVSR AVRRNRAGMG DPNRPVGSFL FLGPTGVGKT ELAKTLAEEL FGEDDRMIRF
DMSEFQEKHT VARLVGAPPG YVGYDEAGQL TEKVRRRPYS VVLFDEVEKA HPDVFNTLLQ
ILDDGRLTDG QGRTVDFRHC VVIMTSNIGA HRILAHKGDV SELKDELMEE LRARFLPEFL
NRIDDIIIFH GLTEGDLGQI VDHLLDRSER RVEAQGMHLE VTEAAKKLLI AHGHQPEFGA
RPLRRTIQAE LDNRVADILL GGEAEPGDTI VADVTDDSLH CTVRKDAPKP DAAAEDKDGN
EES
//