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Database: UniProt
Entry: F5T020_9GAMM
LinkDB: F5T020_9GAMM
Original site: F5T020_9GAMM 
ID   F5T020_9GAMM            Unreviewed;       754 AA.
AC   F5T020;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   SubName: Full=ATPase with chaperone activity, ATP-binding subunit {ECO:0000313|EMBL:EGL54856.1};
GN   ORFNames=MAMP_01850 {ECO:0000313|EMBL:EGL54856.1};
OS   Methylophaga aminisulfidivorans MP.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Methylophaga.
OX   NCBI_TaxID=1026882 {ECO:0000313|EMBL:EGL54856.1, ECO:0000313|Proteomes:UP000003544};
RN   [1] {ECO:0000313|EMBL:EGL54856.1, ECO:0000313|Proteomes:UP000003544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP(T) {ECO:0000313|Proteomes:UP000003544};
RX   PubMed=21685284; DOI=10.1128/JB.05403-11;
RA   Han G.H., Kim W., Chun J., Kim S.W.;
RT   "Draft genome sequence of Methylophaga aminisulfidivorans MP T.";
RL   J. Bacteriol. 193:4265-4265(2011).
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:EGL54856.1}.
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DR   EMBL; AFIG01000001; EGL54856.1; -; Genomic_DNA.
DR   RefSeq; WP_007144742.1; NZ_AFIG01000001.1.
DR   AlphaFoldDB; F5T020; -.
DR   STRING; 1026882.MAMP_01850; -.
DR   eggNOG; COG0542; Bacteria.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000003544; 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:0043335; P:protein unfolding; IEA:InterPro.
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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003544};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..145
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          142..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..166
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   754 AA;  82814 MW;  5217E8D8BF77AA83 CRC64;
     MLSKELEQTL SQAFNYARQR AHEFLTVEHL LLALLENGQA LAVLKACEVD ITVLRQELSD
     FLADNLPTLA EDSERETQPT LAFQRILQRA VMHVQSSGGS EVTGANVLVS IFSEQQSQAV
     YLLQKQDVTR LDVVNAISHG DVEDSAATSE SEAKVESEDV SDDDKSPLTL YAENLNAAAI
     KGKIDPLVGR AHELERTLQI LCRRRKNNPL FVGEAGVGKT ALAEGLARRI VHGDVPEVLA
     ETTIYSLDMG ALVAGTKYRG DFEKRLKALL RELKKQPHAI LFIDEIHTMI GAGSAGNSTM
     DAANLLKPLL ASGELKCIGS TTYQEYRGIF EHDRALARRF QKIDLPEPSV AETIEILKGL
     KPGLEEHHNV RYSNAAIEQA AELAHRHIND RFLPDKAIDV LDEVGAAQRI APKSKRKKLI
     GVNDVQAIVA KIARIPAKTV SNADKDNLRK LEDNLKRVIF GQDEAISALG SAIKMARSGL
     GHPEKPTGAF LFAGPTGVGK TEVTRQLAHN LGVDLIRFDM SEYMESHTVS RLIGAPPGYV
     GFDQGGLLTD AIIKQPHAVL LLDEIEKAHP DVFNLLLQVM DHGTLTDNNG RKADFRHVVL
     VMTSNAGAAE MSKPSIGFTK QDNLTSDGNE ALKRTFTPEF RNRLDGIIQF KPLDKDAILR
     VADKAVLELE MLLEDKNVTI EVNDAARQWL AEHGYDVQMG ARPMARLVQE KIKRPLADEL
     LFGKLSQGGG HVRVTLKDED IHLEMDSAAE AVKS
//
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