ID S5MB49_9MOLU Unreviewed; 598 AA.
AC S5MB49;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Chaperone protein DnaK {ECO:0000256|HAMAP-Rule:MF_00332};
DE AltName: Full=HSP70 {ECO:0000256|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock 70 kDa protein {ECO:0000256|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock protein 70 {ECO:0000256|HAMAP-Rule:MF_00332};
GN Name=dnaK {ECO:0000256|HAMAP-Rule:MF_00332,
GN ECO:0000313|EMBL:AGR40998.1};
GN ORFNames=STAIW_v1c03400 {ECO:0000313|EMBL:AGR40998.1};
OS Spiroplasma taiwanense CT-1.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=1276220 {ECO:0000313|EMBL:AGR40998.1, ECO:0000313|Proteomes:UP000014984};
RN [1] {ECO:0000313|EMBL:AGR40998.1, ECO:0000313|Proteomes:UP000014984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT-1 {ECO:0000313|EMBL:AGR40998.1};
RX PubMed=23873917; DOI=10.1093/gbe/evt108;
RA Lo W.S., Ku C., Chen L.L., Chang T.H., Kuo C.H.;
RT "Comparison of metabolic capacities and inference of gene content evolution
RT in mosquito-associated Spiroplasma diminutum and S. taiwanense.";
RL Genome Biol. Evol. 5:1512-1523(2013).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000256|HAMAP-Rule:MF_00332}.
CC -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000256|HAMAP-
CC Rule:MF_00332}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|HAMAP-Rule:MF_00332,
CC ECO:0000256|RuleBase:RU003322}.
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DR EMBL; CP005074; AGR40998.1; -; Genomic_DNA.
DR RefSeq; WP_020834137.1; NC_021846.1.
DR AlphaFoldDB; S5MB49; -.
DR STRING; 1276220.STAIW_v1c03400; -.
DR KEGG; stai:STAIW_v1c03400; -.
DR PATRIC; fig|1276220.3.peg.343; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_14; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000014984; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR CDD; cd10234; HSPA9-Ssq1-like_NBD; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR HAMAP; MF_00332; DnaK; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR012725; Chaperone_DnaK.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR NCBIfam; TIGR02350; prok_dnaK; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00332}; Chaperone {ECO:0000256|HAMAP-Rule:MF_00332};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00332};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_00332}; Reference proteome {ECO:0000313|Proteomes:UP000014984};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 519..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 175
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 598 AA; 65287 MW; A2A3B3A30729BEB6 CRC64;
MAKEKIIGID LGTTNSCVAV MEGGQPMVLE NPEGQRTTPS VVAFKNSDII IGGAAKRQAV
TNPNTAISIK RDMGTSKKVN LEGKDYTPEQ ISAEILRYLK KYAEDKIGSK ITKAVITVPA
YFNDSQRKAT KDAGKIAGLE VERIINEPTA AALAYGIDKQ DKEMKVLVYD LGGGTFDVSL
LELADGTYDV LATSGDNELG GDDFDKKIMD WIAAGIKKEH SIDLSNDKMA LQRFKDEAEK
AKINLSSQLE TEINLPFIAM NQNGPVNFST KLSRAEFEKM TKDLVERTRK PVEDALKEAK
LKAIEIDQVL LVGGSTRIPA VKELVTSLLG KEPNRTINPD EVVAMGAAIQ GGVLAGDVTD
VLLLDVTPLT LGIETMGGVM TPLIQRNTTI PTEKAQVFST AVDNQPAVDI NVLQGERPMA
GDNKSLGQFQ LTGIKPAPKG VPQIEVTFKI DVNGIVSVTA KDKDTNEEKT ITISNSGSLS
ESEIERMVKE AEENQEADNK KRKNIELKNK AESYLNIIED SSKDSGAQMT DEQKKQSEDL
AKEIRELIAK EDYDTLDKKM TELEQAMKMA SEMAAAQAQQ TQEAKPEENK DQSQEENK
//
