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Database: UniProt
Entry: G4CQZ7_9NEIS
LinkDB: G4CQZ7_9NEIS
Original site: G4CQZ7_9NEIS 
ID   G4CQZ7_9NEIS            Unreviewed;       759 AA.
AC   G4CQZ7;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=ATP-dependent Clp protease, ATP-binding subunit ClpA {ECO:0000313|EMBL:EGZ45782.1};
GN   Name=clpA {ECO:0000313|EMBL:EGZ45782.1};
GN   ORFNames=HMPREF9370_1507 {ECO:0000313|EMBL:EGZ45782.1};
OS   Neisseria wadsworthii 9715.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=1030841 {ECO:0000313|EMBL:EGZ45782.1, ECO:0000313|Proteomes:UP000005336};
RN   [1] {ECO:0000313|EMBL:EGZ45782.1, ECO:0000313|Proteomes:UP000005336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9715 {ECO:0000313|EMBL:EGZ45782.1,
RC   ECO:0000313|Proteomes:UP000005336};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC       involved in the recovery of the cell from heat-induced damage, in
CC       cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the
CC       processing of protein aggregates. Protein binding stimulates the ATPase
CC       activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC       which probably helps expose new hydrophobic binding sites on the
CC       surface of ClpB-bound aggregates, contributing to the solubilization
CC       and refolding of denatured protein aggregates by DnaK.
CC       {ECO:0000256|ARBA:ARBA00025613}.
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:EGZ45782.1}.
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DR   EMBL; AGAZ01000055; EGZ45782.1; -; Genomic_DNA.
DR   RefSeq; WP_009116648.1; NZ_JH165159.1.
DR   AlphaFoldDB; G4CQZ7; -.
DR   STRING; 1030841.HMPREF9370_1507; -.
DR   PATRIC; fig|1030841.3.peg.1489; -.
DR   HOGENOM; CLU_005070_4_1_4; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000005336; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0043335; P:protein unfolding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   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; IPR013461; ClpA.
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   NCBIfam; TIGR02639; ClpA; 1.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF111; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPA; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 1.
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; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 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   Hydrolase {ECO:0000313|EMBL:EGZ45782.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:EGZ45782.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          206..350
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          487..636
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          653..742
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          145..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..168
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   759 AA;  84381 MW;  D86FB5BFC1DD5A3F CRC64;
     MISAELERIL QYIYADARAR GYELISLEHL LLILIEQSDD VHNLLKAVGA DLQLLSSQLM
     NSVVENTPML PQDSMGHIET QPTIGFQRVL QRAIIHAQSA DKQEVLPIDI LVALMGEKEC
     PAVYFLSLQS IGRYEILNCL AHGESHTDST DYRSVSEDTD SKEKDKDDLS SYTVNLNAEV
     SAGRIDPLIG RKHEMERLVQ VLCRRRKNNP LLVGEAGVGK TALAEGLAHQ IVNHQIPETL
     KDAVVFTLDM GALLAGTKYR GDFEARVKTV LKALAEIPNA ILFIDEIHTI IGAGSTSGGT
     MDASNLLKPA LAKGQLRCIG ATTYDEYRTI FDKDHALSRR FQKIDVVEPS VQETVQILRG
     LKPMFEDFHQ VRYTHGALEA AAELSARYIN ERFLPDKAID VVDEAGAAQR ILPKSKQKKV
     IGKAQIEAVI AKVARIPEKT VSHDDKQVLQ YLARDLKNMV FGQDKAIDAL VAAVKMSRSG
     LGQPDKPIGS FLFSGPTGVG KTEVAKQLAF ALGVPLQRFD MSEYMERHAV SRLIGSPPGY
     VGFEQGGLLT EAVNKQPYCV LLLDEIEKAH PDIFNVLLQV MDYGKLTDNN GKSADFRNVI
     IIMTTNAGAE SLSRPTLGFT NQRERGDEMV AINKTFTPEF RNRIDAVIPF APLNEPIVEK
     VVDKFLLQLE KQLLDKKVEV EFTPGLRKYL AEKGFDPQMG ARPMHRLIQD KIRKVLADEL
     LFGKLKDGGF VRIGWDKEKE TVVLKFKKIE QKNRAIADA
//
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