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Database: UniProt
Entry: A0A316CCI6_PSESE
LinkDB: A0A316CCI6_PSESE
Original site: A0A316CCI6_PSESE 
ID   A0A316CCI6_PSESE        Unreviewed;       821 AA.
AC   A0A316CCI6;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:PWJ85777.1};
GN   ORFNames=C7441_102223 {ECO:0000313|EMBL:PWJ85777.1};
OS   Pseudaminobacter salicylatoxidans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Pseudaminobacter.
OX   NCBI_TaxID=93369 {ECO:0000313|EMBL:PWJ85777.1, ECO:0000313|Proteomes:UP000245396};
RN   [1] {ECO:0000313|EMBL:PWJ85777.1, ECO:0000313|Proteomes:UP000245396}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6986 {ECO:0000313|EMBL:PWJ85777.1,
RC   ECO:0000313|Proteomes:UP000245396};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:PWJ85777.1}.
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DR   EMBL; QGGG01000002; PWJ85777.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316CCI6; -.
DR   STRING; 1192868.GCA_000304395_03961; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000245396; 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; 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:PWJ85777.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:PWJ85777.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245396};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..148
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          145..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          757..821
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        757..781
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   821 AA;  89718 MW;  D84EB77DAF353BCB CRC64;
     MPAFSQGLEK ALHQALTFAN ERHHEYATLE HLLLALIDDA EAAAVMRACN VDLDELKHTV
     LTYIDTELDN LVTGYDEDSK PTAGFQRVIQ RAVIHVQSSG RDEVSGANVL VAIFAERESH
     AAYFLQEQQM TRYDAVNYIS HGIAKRPGAS ESRTPRGAED DQSGSAGDAS EDSGKKKQQD
     ALSAYCIDLN KKARAGKIDP LIGRASEINR TIQVLCRRSK NNPLYVGDPG VGKTAIAEGL
     AKRIVEGDVP DVLADATIFA LDMGTLLAGT RYRGDFEERL KQVVKELEEY PGAVLFIDEI
     HTVIGAGATS GGAMDASNLL KPALSSGAIR CIGSTTYKEF RQFFEKDRAL VRRFQKIDVN
     EPTVDDAIEI MKGLRPYYEQ FHRVKYTNDA IKAAVELSAR YISDRKLPDK AIDVIDETGA
     SQMLLPEGKR KKTIGIREIE ATVATMARIP PKTVSADDEQ VLANLETELR RVVYGQDTAI
     TALASAIKLA RAGLREPEKP IGSYLFSGPT GVGKTEVARQ LAASLGVELI RFDMSEYMER
     HTVSRLIGAP PGYVGFDQGG LLTDGVDQHP HCVLLLDEVE KAHPDLFNIL LQVMDHGKLT
     DHNGKQIDFR NVILIMTTNA GAADLAKPAI GFGSSKREGD DMDAINRLFS PEFRNRLDAI
     IPFGSLPVPV VHQVVQKFVM QLEAQLSERG VTFDLSPEAI AWLADKGYDE RMGARPLGRV
     IQEYIKKPLA EEVLFGKLKK GGTVRVTVET GEDGETGLKL DTIADEVPVK PRKENPGKPV
     AKKPAAKKAA AKKTTAQKPK SSPKGKDGAK RSLVPQLPRK G
//
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