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Database: UniProt
Entry: A0A5Q0BBG4_9GAMM
LinkDB: A0A5Q0BBG4_9GAMM
Original site: A0A5Q0BBG4_9GAMM 
ID   A0A5Q0BBG4_9GAMM        Unreviewed;       874 AA.
AC   A0A5Q0BBG4;
DT   22-APR-2020, integrated into UniProtKB/TrEMBL.
DT   22-APR-2020, sequence version 1.
DT   28-JUN-2023, entry version 11.
DE   SubName: Full=AAA domain-containing protein {ECO:0000313|EMBL:QFY41265.1};
GN   ORFNames=F6R98_00420 {ECO:0000313|EMBL:QFY41265.1};
OS   Candidatus Methylospira mobilis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Candidatus Methylospira.
OX   NCBI_TaxID=1808979 {ECO:0000313|EMBL:QFY41265.1, ECO:0000313|Proteomes:UP000325755};
RN   [1] {ECO:0000313|EMBL:QFY41265.1, ECO:0000313|Proteomes:UP000325755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shm1 {ECO:0000313|EMBL:QFY41265.1,
RC   ECO:0000313|Proteomes:UP000325755};
RA   Oshkin I.Y., Dedysh S.N., Miroshnikov K., Danilova O.V., Hakobyan A.,
RA   Liesack W.;
RT   "Ecophysiology of the spiral-shaped methanotroph Methylospira mobilis as
RT   revealed by the complete genome sequence.";
RL   Submitted (SEP-2019) 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; CP044205; QFY41265.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5Q0BBG4; -.
DR   KEGG; mmob:F6R98_00420; -.
DR   InParanoid; A0A5Q0BBG4; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000325755; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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; 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   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 2.
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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000325755};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          3..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          854..874
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          410..487
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   874 AA;  97324 MW;  F023B839550A4479 CRC64;
     MIIEKFNLKA QEAIERACRL AVEKDHGFVT PWHLLFALAE QKNAIGRRYL EQAKIDLTQL
     GVKLDSQLLV LPKALKNNQQ TPINRELERL FILAEQASAR LAEKYIGINH ILLAMWELED
     VAAVLSEAGG NKETSRSQLE QKAPGGYSKT DADSGEFEYL HKYARDLTEM ARQGELDPVI
     GRNEEISLAI QVLCRRIKNN PIIIGEPGVG KTAIVEGLAQ RIIAGDVPKD LQGCSVLAVD
     MGLLIAGAKY RGEFEERFKR LIQEITDAGN ILTFIDEIHT LVGAGKAEGS MDAANLLKPA
     LARGELRCVG ATTIEEYRKY FEKDTALIRR FQVVKVEEQD DEGTMLILRG IKEKYEMHHG
     VHISEAALSA AIRLSRRYIA DRFLPDKAID LIDQTAATVR IGLSAKPPAL EELDRRLVAL
     EIELQSLAHE AAEARKQQLQ IEVAELRAQS VAMTERWERE KRAVTEVQNA RKALESARRE
     MEQKIREEDF VSVAELQHKI IPQAEKVLAE YADLDTSPEG GAVKNSINEE DVAATVARLT
     GIPVSKMLDS EQQRLLNLES HLRERVVGQE EAVAAVSKAI RRARTQIQDA NRPLGSFLML
     GPTGVGKTEL AKTLAQFLFN DEAAMVRIDM SEFMEKHSIA RLTGAPPGYV GYEEGGVLTN
     QLRSKPYTVV LFDEVEKAHQ DVFNLFLQVL DEGRLTDSQG QQVNFSNALI LLTSNLGAEH
     IEPVETEEEH RAMQSLIMES VRGHFRPEFL NRLDDILIFR QLTLETMRPI ADIQLNRLIK
     RLSERDIRLE ISDEAAASLA RWGFNPLYGA RPLKRVIQSR LQDPLAELLL SGAITDGQRV
     SVAVADDELT FHTDAQAGGG AKSDPAQSGG PSML
//
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