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Database: UniProt
Entry: M5TH60_9BACT
LinkDB: M5TH60_9BACT
Original site: M5TH60_9BACT 
ID   M5TH60_9BACT            Unreviewed;       853 AA.
AC   M5TH60;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   SubName: Full=Negative regulator of genetic competence ClpC/mecB {ECO:0000313|EMBL:EMI43103.1};
GN   ORFNames=RRSWK_04404 {ECO:0000313|EMBL:EMI43103.1};
OS   Rhodopirellula sp. SWK7.
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=595460 {ECO:0000313|EMBL:EMI43103.1, ECO:0000313|Proteomes:UP000012028};
RN   [1] {ECO:0000313|EMBL:EMI43103.1, ECO:0000313|Proteomes:UP000012028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SWK7 {ECO:0000313|EMBL:EMI43103.1,
RC   ECO:0000313|Proteomes:UP000012028};
RX   PubMed=23273849;
RA   Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C., Richter M.,
RA   Achstetter T., Glockner F.O., Harder J.;
RT   "Expression of sulfatases in Rhodopirellula baltica and the diversity of
RT   sulfatases in the genus Rhodopirellula.";
RL   Mar. Genomics 0:0-0(2012).
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:EMI43103.1}.
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DR   EMBL; ANOQ01000087; EMI43103.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5TH60; -.
DR   STRING; 595460.RRSWK_04404; -.
DR   PATRIC; fig|595460.3.peg.4801; -.
DR   eggNOG; COG0542; Bacteria.
DR   Proteomes; UP000012028; Unassembled WGS sequence.
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   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..133
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          425..460
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          139..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          816..853
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          421..474
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        154..168
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   853 AA;  94757 MW;  9AD9553F5F679F43 CRC64;
     MQLANQEAQR FNHEYIGTEH ILLGLVKEGS GVAANVLKNL DVDLRKIRLE VEKLVQSGPE
     MVTVGKLPQT PRAKKVIEYS MEEARNLNHS YVGTEHILLG LLREQEGVAA QVLMNLGLKL
     EDVREEVLNL LGHGLEGAEV GERGGRSGEG SDGGGSGGGS SKSGKSKTPA LDSFGRDLTE
     LARKGELDPV IGREREIERA IQILCRRTKN NPVLLGEAGV GKTAIIEGFA QRVINGEVPE
     ILSEKRIVVL DLAMMVAGTK YRGQFEERIK AVMTEVRRVK NTILFIDELH TLVGAGGAEG
     AIDAANVLKP ALARGEIQCI GATTLDEYRK YIEKDNALAR RFQEIMVEPT GTAETIEILK
     GLRERYEEHH RVQFTDDAVV AAVEMSERYI TARCLPDKAI DVIDEAGARV RLRSMTRPPD
     LKEIDEQVET LNKDKEDAVA NQDFEKAANL RDQAEKLRKK KEKITQEWRE KSQQTDGVVD
     EEVIAEVVSK MTGIPLTRLS TEDSLRLLKM EDELHERVVS QEQAVTAIAK AVRRSRSGLK
     DPKRPTGSFI FAGPTGVGKT LLAKALAEYM FGDPDALVHI DMSEYMEKHN VSRLIGAPPG
     FVGYEEGGQL TEKIRRRPYA VVLFDEIEKA HPDVFNMLLQ VMEEGRLTDS FGRNVDFRNT
     ILIMTTNAGA EAIKNEAAFG FAKPDGDASY DSMKSRVMDS IERVFRPEFL NRLDDTIIFR
     HLTTTDLKGI IDFELQKVRE RLLERGLALE LTDDAKEFLV KKGSNLDYGA RPLRRALEQR
     IEDPLGEELL RGTFVGKDTI VIDVHRDDSG KITRLNFEGE TRGLPDPKDS EETVGASAGS
     EGEKPEESSE DKS
//
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