ID Q1QKP1_NITHX Unreviewed; 799 AA.
AC Q1QKP1;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 24-JAN-2024, entry version 112.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:ABE63206.1};
DE EC=3.4.21.92 {ECO:0000313|EMBL:ABE63206.1};
GN OrderedLocusNames=Nham_2416 {ECO:0000313|EMBL:ABE63206.1};
OS Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Nitrobacter.
OX NCBI_TaxID=323097 {ECO:0000313|EMBL:ABE63206.1, ECO:0000313|Proteomes:UP000001953};
RN [1] {ECO:0000313|EMBL:ABE63206.1, ECO:0000313|Proteomes:UP000001953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10229 / NCIMB 13809 / X14
RC {ECO:0000313|Proteomes:UP000001953};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L.,
RA O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T.,
RA Gentry M.E., Bruce D., Richardson P.;
RT "Complete sequence of chromosome of Nitrobacter hamburgensis X14.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP000319; ABE63206.1; -; Genomic_DNA.
DR RefSeq; WP_011510879.1; NC_007964.1.
DR AlphaFoldDB; Q1QKP1; -.
DR STRING; 323097.Nham_2416; -.
DR KEGG; nha:Nham_2416; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_5; -.
DR OMA; GRVIQEH; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000001953; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
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; PS51903; CLP_R; 1.
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:ABE63206.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:ABE63206.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001953};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..149
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 151..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 799 AA; 87978 MW; 562B6382CF0D1B88 CRC64;
MPTFSQSLEQ SLHRALAIAN ERHHQYATLE HLLLSLVDDS DAAAVMRACS VDLDKLRGSL
VNYLETEFEN LVAADAADDA KPTAGFQRVI QRAVIHVQSS GREEVTGANV LIAIFAERES
HAAYFLQEQD MTRYDAVNYI SHGIAKRPGV SEARPVRGVD EETESKSGGD DAKKKGDALE
TYCVNLNKKA RDGKIDPVIG RHAEINRAIQ VLCRRQKNNP LFVGDAGVGK TAIAEGLAKR
IVDSEVPEVL SASTVFSLDM GTLLAGTRYR GDFEERLKQV LKELEAHPNA ILFIDEIHTV
IGAGATSGGA MDASNLLKPA LASGTIRCMG STTYKEYRQH FEKDRALVRR FQKIDVNEPS
VEDAIAILKG LKPYFEDYHK LKYTNDAIEA AVQLSSRYIH DRKLPDKAID VIDESGAAQM
LVSENRRKKT IGIKEIETTI AAMARIPPKS MSKDDAEVLK HLEQTLKRVV FGQDLAIEAL
TAAIKLARAG LREPEKPIGS YLFSGPTGVG KTEVAKQLAA AMGVELLRFD MSEYMERHTV
SRLIGAPPGY VGFDQGGLLT DGVDQHPHCV VLLDEIEKAH PDVYNVLLQI MDHGRLTDHH
GKQVNFRNVI LIMTTNAGAS DMAKAAFGFT RSKREGDDHE AINRQFSPEF RNRLDATVSF
GHLSTDVIGM VVEKFVLQLE AQLADRFVTI ELSEPAKAWL VQHGYDEQMG ARPMARVIQE
HIKKPLADEV LFGKLKGGGH VRVVLVKDEA VAGVDLEKIG FEFLEGPVTP KPEKLPGARR
RPPPRKPKSG GISKEPLKV
//