GenomeNet

Database: UniProt
Entry: M5RC34_9BACT
LinkDB: M5RC34_9BACT
Original site: M5RC34_9BACT 
ID   M5RC34_9BACT            Unreviewed;       859 AA.
AC   M5RC34;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=Negative regulator of genetic competence ClpC/MecB {ECO:0000313|EMBL:EMI17048.1};
GN   ORFNames=RMSM_06023 {ECO:0000313|EMBL:EMI17048.1};
OS   Rhodopirellula maiorica SM1.
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=1265738 {ECO:0000313|EMBL:EMI17048.1, ECO:0000313|Proteomes:UP000011991};
RN   [1] {ECO:0000313|EMBL:EMI17048.1, ECO:0000313|Proteomes:UP000011991}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM1 {ECO:0000313|EMBL:EMI17048.1,
RC   ECO:0000313|Proteomes:UP000011991};
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:EMI17048.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ANOG01000870; EMI17048.1; -; Genomic_DNA.
DR   RefSeq; WP_008704953.1; NZ_ANOG01000870.1.
DR   AlphaFoldDB; M5RC34; -.
DR   PATRIC; fig|1265738.3.peg.6012; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000011991; 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   Reference proteome {ECO:0000313|Proteomes:UP000011991};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          2..145
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          434..469
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          151..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          827..859
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          430..476
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        161..179
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        845..859
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   859 AA;  95918 MW;  412AB130DFAC5908 CRC64;
     MYERFTDRAR KVMQLANQEA QRFNHEYIGT EHILLGLVKE GSGVAANVLK NLEVDLRKIR
     LEVEKLVQSG PEMVTVGKLP QTPRAKKVIE YSMEEARNLN HSYVGTEHIL LGLLREQEGV
     AAQVLMNLGL KLEDVREEVL NLLGHGLEGA EVGERGGRSG DGESSGSSSG KSSKSKTPAL
     DSFGRDLTEL AKKGELDPVI GREREIERAI QILCRRTKNN PVLLGEAGVG KTAIIEGFAQ
     KVIEGEVPEI LAEKRIVVLD LAMMVAGTKY RGQFEERIKA VMTEVRRVKN TILFIDELHT
     LVGAGGAEGA IDAANVLKPA LARGEIQCIG ATTLDEYRKY IEKDNALARR FQEIIVEPTG
     KVETIAILKG LRERYEEHHR VQFTDDAIVA AVEMSERYIT ARCLPDKAID VIDEAGARVR
     LRTMTRPPDL KEIDEEVEKL NKEKEDAVAN QDFEKAANLR DQAEKLRKKK DQITAEWRQK
     SQQTDGVVDE EVIAEVVSKM TGIPLTRLST EDSLRLMKME EELHKRVVSQ EQAVTAVAKA
     VRRSRSGLKD PRRPTGSFIF AGPTGVGKTL LAKALAEYMF GDAEALVHID MSEYMEKHNV
     SRLIGAPPGF VGYEEGGQLT EKIRRRPYAV VLFDEIEKAH PDVFNMMLQV MEEGRLTDSF
     GRNIDFRNTI LIMTTNAGAE AIKNESSFGF QKPDGDASYD SMKSRVMDQI ERVFRPEFLN
     RLDDTIIFRH LTKEDLKSVI DYELSKVRER LLERGLAIEL TDDAKEFLVK KGSNLDYGAR
     PLRRAIEQRI EDPLSEELLQ GAFEGKDTIV IDAFKGSDGK ITRLDFKGEK RGLSEPSETV
     SAGVGEDKGD SEKSEGNDS
//
DBGET integrated database retrieval system