ID A9WUP1_RENSM Unreviewed; 830 AA.
AC A9WUP1;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE SubName: Full=Negative regulator of genetic competence {ECO:0000313|EMBL:ABY24912.1};
GN OrderedLocusNames=RSal33209_3195 {ECO:0000313|EMBL:ABY24912.1};
OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS NBRC 15589 / NCIMB 2235).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Renibacterium.
OX NCBI_TaxID=288705 {ECO:0000313|EMBL:ABY24912.1, ECO:0000313|Proteomes:UP000002007};
RN [1] {ECO:0000313|Proteomes:UP000002007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235
RC {ECO:0000313|Proteomes:UP000002007};
RX PubMed=18723615; DOI=10.1128/JB.00721-08;
RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT reductive evolution away from an environmental Arthrobacter ancestor.";
RL J. Bacteriol. 190:6970-6982(2008).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP000910; ABY24912.1; -; Genomic_DNA.
DR RefSeq; WP_012246554.1; NC_010168.1.
DR AlphaFoldDB; A9WUP1; -.
DR STRING; 288705.RSal33209_3195; -.
DR KEGG; rsa:RSal33209_3195; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_11; -.
DR Proteomes; UP000002007; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; 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; IPR002078; Sigma_54_int.
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; PS50045; SIGMA54_INTERACT_4; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000002007};
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 424..459
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT DOMAIN 517..782
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
SQ SEQUENCE 830 AA; 91446 MW; AC36ABF38BFC4026 CRC64;
MFERFTDRAR RVVVLAQEEA RMLNHNYIGT EHILLGLIHE GEGIAAKALE SLSISLDAVR
EQVQEIIGQG QQAPSGHIPF TPRAKKVLEL SLREALQLGH NYIGTEHILL GLIREGEGVA
AQVLVKLGAD LSRVRQQVIQ LLSGYQGKET ASAGVGQGQQ EGTPAGSVVL DQFGRNLTQD
ARDNKLDPVI GREHEMERVM QILSRRTKNN PVLIGEPGVG KTAVVEGLAQ AIARGDVPDT
IKDKQLYTLD LGSLVAGSRY RGDFEERLKK VLKEIQTRGD IILFIDEIHT LVGAGAAEGA
IDAASILKPK LARGELQTIG ATTLDEYRKH IEKDAALERR FQPIQVKEPS VSHAIEILKG
LRDRYEAHHR VSITDGALTS AATLAERYIS DRFLPDKAID LIDEAGARLR IRRMTAPPEL
KEMDGEIASV KAQKEAAIDA QDFEGAAALR DTEQKLITER ADKDRAWRTG GIDSVTEVDE
ELIAEVLANS TGIPVFKLTE EESGRLLKME DELHKRVVGQ DEAIKSLSQA IRRTRAGLKD
PKRPGGSFIF AGPTGVGKTE LAKALAEFLF GEEDALITLD MSEYSEKHTV SRLFGAPPGY
VGYEEGGQLT EKVRRRPFSV VLFDEVEKAH ADLFNSLLQI LEDGRLTDSQ GRVVDFKNTV
IIMTTNLGTR DISKSVATGF QSGTDTQTGY NRMRARVTEE LKQHFRPEFL NRVDDVVVFP
QLTQDEIVEI VDMFVARLEL RLKEKDMGIE LTAAAKALLA TRGYDPAMGA RPLRRTIQRE
IEDQLSEKIL FGELKAGEIV VVDVEGDGDE AKFTFAGTAK PRVPEIAPVA
//
