ID M2WG25_9MICC Unreviewed; 884 AA.
AC M2WG25;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=ATP-dependent Clp protease {ECO:0000313|EMBL:EME37482.1};
GN ORFNames=C884_01533 {ECO:0000313|EMBL:EME37482.1};
OS Kocuria palustris PEL.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=1236550 {ECO:0000313|EMBL:EME37482.1, ECO:0000313|Proteomes:UP000009877};
RN [1] {ECO:0000313|EMBL:EME37482.1, ECO:0000313|Proteomes:UP000009877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEL {ECO:0000313|EMBL:EME37482.1,
RC ECO:0000313|Proteomes:UP000009877};
RX PubMed=24504000;
RA Sharma G., Khatri I., Subramanian S.;
RT "Draft Genome Sequence of Kocuria palustris PEL.";
RL Genome Announc. 2:e01261-13(2014).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {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:EME37482.1}.
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DR EMBL; ANHZ02000003; EME37482.1; -; Genomic_DNA.
DR RefSeq; WP_006213590.1; NZ_ANHZ02000003.1.
DR AlphaFoldDB; M2WG25; -.
DR STRING; 71999.KPaMU14_01605; -.
DR Proteomes; UP000009877; 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; -; 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:SF193; CHAPERONE PROTEIN CLPB; 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 Hydrolase {ECO:0000313|EMBL:EME37482.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:EME37482.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009877};
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 427..462
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 145..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 884 AA; 97154 MW; B8EC57E6774F4F38 CRC64;
MFERFTDRAR RVVVLAQEEA RMLNHNYIGT EHLLLGLIHE NEGVAAKALD SLGITLNGAR
EQVQDIIGPG QQAPSGHIPF TPRAKKVLEL SLREALQLGH NYIGTEHILL GIIRAGEGVA
AQVLTKLGTE PQKVRSTVLD LISGYQSGGE EKETAGAGAR TSGEGTPAGS AVLDQFGRNL
TAAARESQLD PVIGRAREME RVMQVLSRRT KNNPVLIGEP GVGKTAVVEG LAQAIVRGDV
PETLKDKHLY TLDLGSLVAG SRYRGDFEER LKKVLKEIKS RGDIILFIDE IHTLVGAGAA
EGAIDAASIL KPMLARGELQ TIGATTLDEY RKHIEKDAAL ERRFQPIQVD EPSEAHSIEI
LKGLRDKYEA HHRVSISDEA LEAAVHQSAR YISDRFLPDK AIDLIDEAGA RLRIKRMTAP
PEIKELDERI AKVKQAKEEA IEGQDYEKAA SLRDQEQKLL SERDDKDTAW REGGDQVAEV
TPDVISDVLS AATGVPLYRL TDEESGRLIR MEEELHKRVV GQEEAIKALS RSIRRTRAGL
KDPKRPGGSF IFAGPTGVGK TELARSLAEF LFGDEDSLIT LDMSEYQEKH TVSRLFGAPP
GYVGFEEGGQ LTEKVRRKPF SVVLFDEVEK AHQDLFNSLL QILEDGRLTD SQGRVVDFKN
TVIIMTTNLG TRDISRSVPM GFQAGNDSTT NYERMQQRVN DELKEHFRPE FLNRVDEIVV
FPQLEEKEIV QIVDLFVARL QERLREQDMS IVVSDAAKKV LAKRGYDPTM GARPLRRTIQ
REIEDTLSEK ILFGDIKEGE RVSVDVDGDG DDAKLTFSSV AMSELPDTEF SDDDQDGSAQ
DPDLVPGEVP SGTNVPHSTD GDTGSAGAEA PEPGHGPESG PATA
//
