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
//