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Database: UniProt
Entry: A0A0G3EKQ8_9BACT
LinkDB: A0A0G3EKQ8_9BACT
Original site: A0A0G3EKQ8_9BACT 
ID   A0A0G3EKQ8_9BACT        Unreviewed;       819 AA.
AC   A0A0G3EKQ8;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Negative regulator of genetic competence ClpC/MecB {ECO:0000313|EMBL:AKJ65340.1};
GN   Name=clpC {ECO:0000313|EMBL:AKJ65340.1};
GN   ORFNames=L21SP4_02108 {ECO:0000313|EMBL:AKJ65340.1};
OS   Kiritimatiella glycovorans.
OC   Bacteria; Kiritimatiellota; Kiritimatiellia; Kiritimatiellales;
OC   Kiritimatiellaceae; Kiritimatiella.
OX   NCBI_TaxID=1307763 {ECO:0000313|EMBL:AKJ65340.1, ECO:0000313|Proteomes:UP000035268};
RN   [1] {ECO:0000313|Proteomes:UP000035268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L21-Fru-AB {ECO:0000313|Proteomes:UP000035268};
RA   Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT   "Description and complete genome sequence of the first cultured
RT   representative of the subdivision 5 of the Verrucomicrobia phylum.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AKJ65340.1, ECO:0000313|Proteomes:UP000035268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L21-Fru-AB {ECO:0000313|EMBL:AKJ65340.1,
RC   ECO:0000313|Proteomes:UP000035268};
RX   PubMed=27300277; DOI=10.1038/ismej.2016.84;
RA   Spring S., Bunk B., Sproer C., Schumann P., Rohde M., Tindall B.J.,
RA   Klenk H.P.;
RT   "Characterization of the first cultured representative of Verrucomicrobia
RT   subdivision 5 indicates the proposal of a novel phylum.";
RL   ISME J. 10:2801-2816(2016).
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DR   EMBL; CP010904; AKJ65340.1; -; Genomic_DNA.
DR   RefSeq; WP_052882580.1; NZ_CP010904.1.
DR   AlphaFoldDB; A0A0G3EKQ8; -.
DR   STRING; 1307763.L21SP4_02108; -.
DR   KEGG; vbl:L21SP4_02108; -.
DR   PATRIC; fig|1609981.3.peg.2192; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000035268; Chromosome.
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; 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; PS50151; UVR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035268};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..145
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          429..464
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          144..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          425..452
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        156..171
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   819 AA;  91644 MW;  32AB28A61C3DC107 CRC64;
     MNNFTPRAQK VLQAARAEAE RFNHGYVGTE HILLGLIGLD QGVAVSVLKS MGVELETLRM
     EVEKAVGTGP EMKTIGNIPF TPRAKKVLAL AGREAQSLGH TYVGTEHILL GLLREGEGVA
     ARVLESLGID LEESRMAVMK ELDPNYEPGD EEEAPGPELG TARKEKKGKS KTPALNAFGL
     DLTEEARKGE LDPVIGRKEE IERVIQILCR RTKNNPVLLG EAGVGKTAIA EGLAQNIVEG
     EVPDLLTNRK VVKLDLALMV AGTKYRGQFE ERIKAVMDEI RRMGNIILFL DELHTIVGAG
     SAEGAMDAAN IIKPSLSRGE LQCIGATTLK EYRRFVEKDA ALERRFQSIT VKEPTIEETV
     EILRGLRSKY EEHHHARFSD EALKAAAELS ARYLPDRFLP DKAIDLIDEA GARGRITTMT
     RPPEIRKLED EIEEARRNKD QAIQDQNFEE AASWRDRERG AKEKLDEVVN EWRREREENT
     ISIDDEEIKV VVSKWTGVPV AKMGEAEMKK LLEMEDTLSR VVIGQDEAIT AIARSLRRSR
     ADLKDPTRPI GSFIFLGPTG VGKTMLAKEL ARFVFDDEDA LIQLDMSEYM EKFNVSRLVG
     SPPGYVGHEE GGQLTERVRR RPYSVVLFDE VEKAHPDVMH MLLQILEEGR LTDSLGRSVD
     FRNTVIIMTS NLGGELVKKG GGMGFGQISG EMDYAKLKDT MLSEARNVFK PELINRLDDI
     VVFRKLNRTH IERILDNEVE RVRTRLAGRK VDLRLADSAK EYLIEKGFDP TYGARQMRRT
     VEREVEDRLA DAILRGRLED AETVEARAGK EGIEFVPVG
//
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