ID Q7NIW8_GLOVI Unreviewed; 819 AA.
AC Q7NIW8;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 24-JAN-2024, entry version 127.
DE SubName: Full=Endopeptidase Clp ATP-binding chain {ECO:0000313|EMBL:BAC90005.1};
GN OrderedLocusNames=glr2064 {ECO:0000313|EMBL:BAC90005.1};
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221 {ECO:0000313|EMBL:BAC90005.1, ECO:0000313|Proteomes:UP000000557};
RN [1] {ECO:0000313|EMBL:BAC90005.1, ECO:0000313|Proteomes:UP000000557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421 {ECO:0000313|Proteomes:UP000000557};
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
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}.
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DR EMBL; BA000045; BAC90005.1; -; Genomic_DNA.
DR RefSeq; NP_925010.1; NC_005125.1.
DR RefSeq; WP_011142062.1; NC_005125.1.
DR AlphaFoldDB; Q7NIW8; -.
DR STRING; 251221.gene:10759557; -.
DR EnsemblBacteria; BAC90005; BAC90005; BAC90005.
DR KEGG; gvi:glr2064; -.
DR PATRIC; fig|251221.4.peg.2099; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_3; -.
DR InParanoid; Q7NIW8; -.
DR OMA; ERMKAVM; -.
DR OrthoDB; 9803641at2; -.
DR PhylomeDB; Q7NIW8; -.
DR Proteomes; UP000000557; Chromosome.
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:UP000000557};
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 819 AA; 91137 MW; 3F371426F3E9C5D2 CRC64;
MFERFTEKAI KVIMLAQEEA RRLGHNFVGT EQILLGLIGE GTGVAAKVLK SMGVNLKDAR
IEVEKIIGRG SGFVAVEIPF TPRAKRVLEL SLEEARQLGH NYIGTEHLLL GLIREGEGVA
ARVLENLGVD LSKVRTQVIR MLGETAEVSA GGNTGRTKTP TLDEFGSNLT QMAAEGKLDP
VVGREKEIER VIQILGRRTK NNPVLIGEPG VGKTAIAEGL AQRISNNDIP DILADKRVVT
LDIGLLVAGT KYRGEFEERL KKIMDEIRAA GNVVLVIDEV HTLIGAGAAE GAIDAANILK
PALARGELQC IGATTLDEYR KHIERDAALE RRFQPVMVGE PTVDETIEIL RGLRERYEQH
HKLKITDEAL IAAAQLSDRY ISDRYLPDKA IDLVDEAGSR VRLLSSQLPP AAKELDKELR
QILKEKDDAV RGQDYERAGE LRDREMEIKS QIRSIAQARK SETANEESPN VTEEDIAYIV
SSWTGVPVSK LTESETEKLL HMEDVLHQRL IGQEEAVKAI SRAIRRARVG LKNPKRPIAS
FIFSGPTGVG KTELAKSLAT YFFGSEDAMI RLDMSEYMER HTVSKLIGSP PGYVGYNEGG
QLTEAVRRRP YTVILFDEIE KAHPDVFNVL LQILEDGRLT DAKGRTVDFK NTLMIMTSNV
GSKVIEKGGG GLGFNTAGTE EEQRYNRISE LVKEELKQYF RPEFLNRLDE IIVFHPLTRE
EVKQIAVIML REVFARLEEQ NMKIEITDAF NRKLIEEGYS ATYGARPLRR AIQRMLEDQL
AEEILAARLK EGDTVLVDVD SDGKPTFIVK DRTLATAEG
//