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Database: UniProt
Entry: S3YDU3_9MICO
LinkDB: S3YDU3_9MICO
Original site: S3YDU3_9MICO 
ID   S3YDU3_9MICO            Unreviewed;       836 AA.
AC   S3YDU3;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF1484_01430 {ECO:0000313|EMBL:EPH15793.1};
OS   Dermabacter sp. HFH0086.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC   Dermabacter.
OX   NCBI_TaxID=1203568 {ECO:0000313|EMBL:EPH15793.1, ECO:0000313|Proteomes:UP000014577};
RN   [1] {ECO:0000313|EMBL:EPH15793.1, ECO:0000313|Proteomes:UP000014577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HFH0086 {ECO:0000313|EMBL:EPH15793.1,
RC   ECO:0000313|Proteomes:UP000014577};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA   Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Dermabacter sp. HFH0086.";
RL   Submitted (MAY-2013) 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:EPH15793.1}.
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DR   EMBL; ATFO01000007; EPH15793.1; -; Genomic_DNA.
DR   RefSeq; WP_016664339.1; NZ_KE340308.1.
DR   AlphaFoldDB; S3YDU3; -.
DR   STRING; 1203568.HMPREF1484_01430; -.
DR   PATRIC; fig|1203568.3.peg.1407; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_11; -.
DR   Proteomes; UP000014577; 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   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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014577};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          2..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          422..457
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   COILED          418..464
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   836 AA;  91994 MW;  C411E8585DB3045A CRC64;
     MFERFTDRAR RVIVLAQDEA RLLNHNYIGT EHILLGLIHE GEGVGAKALE SLGITLEGVR
     EQVREIITEG TQAPTGHIPF TPRAKKVLEL SLREALQLGH GYIGTEHILL GLLREGDGVA
     VKVLTRMGAQ PAAVRQEVIE RLSGYQGKET VNAGGGNQEG TPSGSLVLDQ FGRNLTQAAR
     DQELDPVIGR EREAERVMQV LSRRTKNNPV LIGEPGVGKS AVVEGLAQSI VAGDVPETLK
     DKQLYTLDLG SLVAGSRYRG DFEERLKKVL KEIKTRGDIV LFIDEIHTLV GAGAAEGAID
     AANILKPMLA RGELQTIGAT TLEEYRKHIE KDAALERRFQ PIQVEEPSVE ETIDILRGLR
     DRYESFHKVT ITDDALEAAA QLAARYVNDR FLPDKAIDLI DEAGARLRIR RLSAPPELKE
     YDQKIEEAKR AKESAIDAQD FEKAASLRDD EQKLTAERKA KEDAWRNGES DSISVVNDDV
     IAEVLAAATG IPIVKLNEAE STRLLNMENE LHKRVVGQNE AIKALSQSIR RTRAGLKDPK
     RPGGSFIFAG PTGVGKTELA KALAEFLFGD EDALITLDMS EFGEKHTASR LFGSPPGYVG
     YDEGGQLTEK VRRKPFSVVL FDEIEKAHVD IFNSLLQILE DGRLTDSQGR VVDFKNTVII
     MTTNLGTRDI AKGVSIGFQA GGDLSTSYER MKAKVNEELK QHFRPEFLNR VDDIVVFPQL
     SREEIAQIVD LMVGRLDTRL AERGMSVTLT PQARTLLAEK GYDPVLGARP LRRAIQRDIE
     DALSEKILFG QVKDGDEIVI DAEGEGPLGI FTFATKNAEG ELEPISEDIS VEDIAG
//
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