ID A0A1Y4SKA0_9FIRM Unreviewed; 587 AA.
AC A0A1Y4SKA0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Chaperone protein DnaK {ECO:0000256|ARBA:ARBA00014415};
DE AltName: Full=Chaperone protein dnaK {ECO:0000256|ARBA:ARBA00017249};
DE AltName: Full=HSP70 {ECO:0000256|ARBA:ARBA00033103};
DE AltName: Full=Heat shock 70 kDa protein {ECO:0000256|ARBA:ARBA00030945};
DE AltName: Full=Heat shock protein 70 {ECO:0000256|ARBA:ARBA00030019};
GN ORFNames=B5E79_07465 {ECO:0000313|EMBL:OUQ29421.1};
OS Massilimicrobiota sp. An134.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Massilimicrobiota.
OX NCBI_TaxID=1965557 {ECO:0000313|EMBL:OUQ29421.1, ECO:0000313|Proteomes:UP000195713};
RN [1] {ECO:0000313|Proteomes:UP000195713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An134 {ECO:0000313|Proteomes:UP000195713};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000256|ARBA:ARBA00002290}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
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:OUQ29421.1}.
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DR EMBL; NFLH01000015; OUQ29421.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4SKA0; -.
DR Proteomes; UP000195713; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR CDD; cd10234; HSPA9-Ssq1-like_NBD; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00012; HSP70; 2.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000195713};
KW Stress response {ECO:0000256|ARBA:ARBA00023016}.
SQ SEQUENCE 587 AA; 64265 MW; 4434A15D6B5EABDE CRC64;
MSKIIGIDLG TTNSCMSFIE NGKTTIIPNS EGAKTTPSVV AFTHDGQRLV GESAKRQAVT
NPMGTISSIK REMGTDYKKK IGNREYTPQE ISAMILQKLK IDAENYLGEE VKQAVITVPA
YFNDAQRQAT KDAGRIAGLE VMRIINEPTA AALAYGLENS YGQKMMVFDL GGGTFDVSII
EIGNGVIEVL STSGDNHLGG DDFNELLAQH ILTEFEKSSG ISLRNDLMAM QRIKEAAEKA
KIELSSMTST VVSLPFITTT SAGPQNLEMT ITRDLFNRMT RELVERTILP MQNALNDARL
LPAELNKIIL VGGSSRIPAV QDKIKEVTGI TPSKSLNPDE CVAMGAGIQG GKLSGDVTAM
GNYDVLLLDV TPLTLSIETV GGVATPLIDR NTPIPTSHSQ IFTTSSNFQT QVEINVLQGE
RPLAKDNKSL GKFKLKKIKR AMRGIPQIEV TFDIDVNGIV SVSAKDLASG NMQSITIENG
SHMSDEDIER AIHEAKQFEQ QDAKTKERLV FKNDLETLMS RVEASLAKHH KEIDKTVRTQ
IKNELNQLKK LTKKVQFETC PDAQFQEIKE AKQRLEDSAA FLLSMGE
//
