ID A0A2W1JHY9_9CYAN Unreviewed; 824 AA.
AC A0A2W1JHY9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Negative regulator of genetic competence ClpC/MecB {ECO:0000313|EMBL:PZD73150.1};
GN Name=clpC_2 {ECO:0000313|EMBL:PZD73150.1};
GN ORFNames=C1752_02280 {ECO:0000313|EMBL:PZD73150.1};
OS Acaryochloris thomasi RCC1774.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC Acaryochloridaceae; Acaryochloris; Acaryochloris thomasi.
OX NCBI_TaxID=1764569 {ECO:0000313|EMBL:PZD73150.1, ECO:0000313|Proteomes:UP000248857};
RN [1] {ECO:0000313|EMBL:PZD73150.1, ECO:0000313|Proteomes:UP000248857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC1774 {ECO:0000313|EMBL:PZD73150.1,
RC ECO:0000313|Proteomes:UP000248857};
RX PubMed=29904088; DOI=10.1038/s41598-018-27542-7;
RA Partensky F., Six C., Ratin M., Garczarek L., Vaulot D., Probert I.,
RA Calteau A., Gourvil P., Marie D., Grebert T., Bouchier C., Le Panse S.,
RA Gachenot M., Rodriguez F., Garrido J.L.;
RT "A novel species of the marine cyanobacterium Acaryochloris with a unique
RT pigment content and lifestyle.";
RL Sci. Rep. 8:9142-9142(2018).
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, 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:PZD73150.1}.
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DR EMBL; PQWO01000006; PZD73150.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W1JHY9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000248857; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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:SF155; CLP PROTEASE ATP-BINDING SUBUNIT; 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 Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000248857};
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 416..451
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
SQ SEQUENCE 824 AA; 91702 MW; 0C0F26F9EBEB3FFC CRC64;
MFERFTEKAI KVIMLAQEEA RRLGHNFVGT EQILLGLIGE GTGVAAKVLK SMGVNLKDAR
VEVEKIIGRG SGFVAVEIPF TPRAKRVLEL SLEEARQLGH NYIGTEHLLL GLIREGEGVA
ARVLENLGVD LGKVRTQVIR MLGETAEVTA GGSSGRTKTP TLDEFGSNLT QLAADGKLDP
VVGRQKEIER VIQILGRRTK NNPVLIGEPG VGKTAIAEGL AQRITNADIP DILEEKRVVT
LDIGLLVAGT KYRGEFEERL KKIMDEIRQA SNVILVIDEV HTLIGAGAAE GAIDAANILK
PALARGELQC IGATTLDEYR KHIERDAALE RRFQPVMVGE PSVDETIEIL YGLRERYEQH
HKLKILDESL EAAAKLSDRY ISDRYLPDKA IDLIDEAGSR VRLINSQLPP AAKELDKELR
QVLKDKDDAV RSQDFDKAGG LRDREMEIKS EIKTIAQAKR DEGSESGGDE SPKVTEEDIA
HIVASWTGVP VNKLTETESD KLMHMEDTLH QRLIGQEEAV KAISRAIRRA RVGLKNPNRP
IASFIFSGPT GVGKTELTKA LATYFFGSED AMVRLDMSEY MERHTVSKLI GSPPGYVGYN
EGGQLTEAVR RRPYTVVLFD EIEKAHPDVF NMLLQILEDG RLTDAKGRTV DFKNTMLIMT
SNIGSKVIEK GGGGLGFDFA EDQVDSQYNR IRSLVNEELK QYFRPEFLNR LDEIIVFRQL
TKDEVKDISE ILLKEVFARL EEKEISLQIT ERFKELLIEE GYNPSYGARP LRRAIMRLLE
DTLAEEILSG RVKAGDTAVV DVNEEGKVHV EPSERRELLP QAVE
//