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Database: UniProt
Entry: A0A2P1PS38_9GAMM
LinkDB: A0A2P1PS38_9GAMM
Original site: A0A2P1PS38_9GAMM 
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
//
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