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Database: UniProt
Entry: A0A0M2RDI4_9PROT
LinkDB: A0A0M2RDI4_9PROT
Original site: A0A0M2RDI4_9PROT 
ID   A0A0M2RDI4_9PROT        Unreviewed;       766 AA.
AC   A0A0M2RDI4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Clp protease ClpX {ECO:0000313|EMBL:KKJ78519.1};
GN   Name=clpA {ECO:0000313|EMBL:KKJ78519.1};
GN   ORFNames=WH95_03360 {ECO:0000313|EMBL:KKJ78519.1};
OS   Kiloniella litopenaei.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Kiloniellaceae; Kiloniella.
OX   NCBI_TaxID=1549748 {ECO:0000313|EMBL:KKJ78519.1, ECO:0000313|Proteomes:UP000034491};
RN   [1] {ECO:0000313|EMBL:KKJ78519.1, ECO:0000313|Proteomes:UP000034491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1-1 {ECO:0000313|EMBL:KKJ78519.1,
RC   ECO:0000313|Proteomes:UP000034491};
RA   Shao Z., Wang L., Li X.;
RT   "Genome sequence of Kiloniella sp. P1-1, isolated from the gut microflora
RT   of Pacific white shrimp, Penaeus vannamei.";
RL   Submitted (MAR-2015) 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:KKJ78519.1}.
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DR   EMBL; LANI01000002; KKJ78519.1; -; Genomic_DNA.
DR   RefSeq; WP_046503354.1; NZ_LANI01000002.1.
DR   AlphaFoldDB; A0A0M2RDI4; -.
DR   STRING; 1549748.WH95_03360; -.
DR   PATRIC; fig|1549748.8.peg.1275; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000034491; 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:KKJ78519.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KKJ78519.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034491};
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          744..766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   766 AA;  84979 MW;  327DB50AE4E30AED CRC64;
     MLSNNLEQTL HRALAYANER RHEYATLEHL LLSLTEDQDG ISVFRACGVE IETLREDLLD
     YIDNDLSNLT TIHLGDAKPT AGFQRVLQRA AIHVQSSGRE EVTGANVLVA MFSERESHAV
     FFLQEQEMSR LDAVNYISHG ITKVEGLEET RTIHGTDDLM EDGESTAAKG REAIDAYCVD
     LNQKAKDGKI DLLVGREQEL ERTIQVLCRR TKNNPLYVGD PGVGKTAIAE GLAKKIVEGE
     VPEVLKETKI FALDMGSLLA GTRYRGDFEE RLKGVVKEIE AMDGAVLFID EIHTVIGAGA
     TSGGSMDASN LLKPALQNGE LSCIGSTTYK EYRNHFEKDR ALVRRFQKID VAEPSIEDAV
     KILRGLKPYY EEHHAVKYSN EALRTAVELS ARYIGDRKLP DKAIDVIDEV GASQMLLPED
     KRKKSLGVKD VEAVVAKIAR IPPKSVSKDD KSVLKNLERD LKTMVYGQDQ VITSLASAIK
     LARAGLRTPE KPIGCYLFTG PTGVGKTEVA KQLSHSLGVE LTRFDMSEYM ERHAVSRLIG
     APPGYVGFDQ GGLLTDAIDK TPHCILLLDE IEKAHPDIFN ILLQVMDNGR LTDNNGKTID
     FRNVILIMTS NAGAADMAKP AIGFGREVRI GDDEEAVNKI FTPEFRNRLD AIIPFKNLSP
     VVMAKVVDKF IMELETQLAD RQVTFELSPK AKKWLATEGY DPLYGARPLA RVIQNEIKKP
     LAEELLFGKL TRGGVVRIDI KDNKPSFSFP EEKKSGPKKS RRKQKA
//
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