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Database: UniProt
Entry: E3FPT9_STIAD
LinkDB: E3FPT9_STIAD
Original site: E3FPT9_STIAD 
ID   E3FPT9_STIAD            Unreviewed;       761 AA.
AC   E3FPT9;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 70.
DE   SubName: Full=ATP-dependent Clp protease, ATP-binding subunit ClpA {ECO:0000313|EMBL:ADO74457.1};
GN   Name=clpA {ECO:0000313|EMBL:ADO74457.1};
GN   OrderedLocusNames=STAUR_6700 {ECO:0000313|EMBL:ADO74457.1};
OS   Stigmatella aurantiaca (strain DW4/3-1).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Archangiaceae; Stigmatella.
OX   NCBI_TaxID=378806 {ECO:0000313|EMBL:ADO74457.1, ECO:0000313|Proteomes:UP000001351};
RN   [1] {ECO:0000313|EMBL:ADO74457.1, ECO:0000313|Proteomes:UP000001351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO74457.1,
RC   ECO:0000313|Proteomes:UP000001351};
RX   PubMed=21037205; DOI=10.1093/molbev/msq292;
RA   Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA   Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA   Sogaard-Andersen L.;
RT   "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL   Mol. Biol. Evol. 28:1083-1097(2011).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; CP002271; ADO74457.1; -; Genomic_DNA.
DR   RefSeq; WP_013377443.1; NZ_AAMD01000086.1.
DR   AlphaFoldDB; E3FPT9; -.
DR   STRING; 378806.STAUR_6700; -.
DR   KEGG; sur:STAUR_6700; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_2_7; -.
DR   OMA; GRVIQEH; -.
DR   OrthoDB; 5477619at2; -.
DR   Proteomes; UP000001351; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:ADO74457.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:ADO74457.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          3..148
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          149..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          7..68
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        149..171
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   761 AA;  83711 MW;  F7FEBB72E7AABB3B CRC64;
     MAGPQIAKEL QTSFRKALEE ARRMQHEYLT LEHLLLALTK DARTREVLKG CGANVKRLEE
     RLEAFLEETV ERLPEDAEGE PQQTIGVERV LHRAAMHALS AEQKVIDGGD VLVALFREDE
     SQALYFLQQE GVTRLDLLNF ISHGITKEGA SDKGEARGVP AGDDDEGEGP RKSPLQAYTT
     LLNTEAKEGR IDPLIGREKE LERTIQVLCR RRKNNPLYVG ETGVGKTAIA EGLALRIHED
     KIPAALKGAE VYSLDMGALL AGTKFRGQFE ERLKGVLKEL QEHPNAILFI DEIHTIVGAG
     ATSGGSMDAS NLLKPALANG RLRCIGSTTY QEFKASFERD RALSRRFQKI EVPEPSVEDT
     VLILEGLKSR YEDHHGVKYD TDALRAAAEL SAKHINDRFL PDKAIDVIDE SGAAERLKPE
     GQRTGKVTMA DVEAVVAKMA RIPAKSVSAQ EGVQLQNLEK ELRAVIFGQD EAIQNLTSTI
     KLARSGLRSP EKPIGSFLFS GPTGVGKTEL AKQLAAVLGV EFLRFDMSEY SEKHTVSRLI
     GAPPGYVGFD QGGLLTDAIR KHPYAVLVLD EIEKAHPDLF NILLQVMDHA TLTDNNGRKA
     DFRNIILILT TNAGAREMNV QAIGFGDTQL PSDPKRAKKA IERTFTPEFR NRLDGWLLFG
     GLSSEVILKV VDKEVGLLQK MLIEKNVKLE LTTAARAWLA EHGYDPAFGA RPMARLVDNR
     LKKPLAEAIL FGELKHGGTA LFDVEGEELT LKPVPLPAAK A
//
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