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Database: UniProt
Entry: A0A1H4L879_9ACTN
LinkDB: A0A1H4L879_9ACTN
Original site: A0A1H4L879_9ACTN 
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
//
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