ID A0A2P1PS38_9GAMM Unreviewed; 762 AA.
AC A0A2P1PS38;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:AVP97648.1};
GN Name=clpA {ECO:0000313|EMBL:AVP97648.1};
GN ORFNames=C7S18_10750 {ECO:0000313|EMBL:AVP97648.1};
OS Ahniella affigens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Ahniella.
OX NCBI_TaxID=2021234 {ECO:0000313|EMBL:AVP97648.1, ECO:0000313|Proteomes:UP000241074};
RN [1] {ECO:0000313|EMBL:AVP97648.1, ECO:0000313|Proteomes:UP000241074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D13 {ECO:0000313|EMBL:AVP97648.1,
RC ECO:0000313|Proteomes:UP000241074};
RA Ko Y., Kim J.-H.;
RT "Ahniella affigens gen. nov., sp. nov., a gammaproteobacterium isolated
RT from sandy soil near a stream.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AVP97648.1, ECO:0000313|Proteomes:UP000241074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D13 {ECO:0000313|EMBL:AVP97648.1,
RC ECO:0000313|Proteomes:UP000241074};
RA Keele B.F.;
RL Submitted (MAR-2018) 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; CP027860; AVP97648.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P1PS38; -.
DR KEGG; xba:C7S18_10750; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000241074; Chromosome.
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; 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:AVP97648.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AVP97648.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000241074};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 144..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 762 AA; 84358 MW; AD3C398B8D1A1A51 CRC64;
MFSKDLEQTL AQCYKDARER RHEFMTVEHL LLALLDNASA ANVLRACGAD FKKLTQDLRS
IIAETVQVMP QGDSRDTQPT LGFQRVLQRA VYHVQSSGRS EVTGANVLVA IFGEKDSHAV
YFLNQQEITR LDVVNYISHR IAKIGHEPKN PEPESKNPNP ADPEGENELR GNPLTEFANN
LNEAARLGKI DPLIGRSDEV ERTIQVLCRR RKNNPLFVGE AGVGKTAIAE GLAKRIVEGQ
VPEVLKDCTI HALDLGALVA GTKYRGDFEK RLKAVIAELK KDPKAILFID EIHTIIGAGS
ASGGTMDASN LIKPVLSSGE LRCIGSTTFQ EFRQIFDKDR ALSRRFQKID IVEPSMADAL
EILKGLKPRF EEHHNIVYTQ DALKAAVDLS VKHIGDRLLP DKAIDVIDEA GARQRVVPEG
ERKDIVDVGE IEYIIAKMAR IPPKQVSVSD REVLKNLDRN LKMVVFGQDD AIDSLTASIK
MARSGLANAG KPIGCFLFAG PTGVGKTEVT RQLALQLGIE LIRFDMSEYM EAHSVSRLIG
APPGYVGFDK GGLLTDAVTK HPHSVILLDE IEKAHPDVFN ILLQVMDRGA LTDSNGREAT
FRNAVLIMTT NAGAAQASRR TIGFVRQDHS TDAMETITKM FSPEFRNRLD TIIQFRALDF
DHILRVVDKF LIELEAQLHD KRVSLSADSE ARRWLAEHGF DPQMGARPMS RVLQEKVKRP
LADELLFGKL SQGGRVHLSV QNGELQIETE AEPIAEAELA ES
//