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Database: UniProt
Entry: B1C311_9FIRM
LinkDB: B1C311_9FIRM
Original site: B1C311_9FIRM 
ID   B1C311_9FIRM            Unreviewed;       586 AA.
AC   B1C311;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Chaperone protein DnaK {ECO:0000256|ARBA:ARBA00014415, 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:EDS74569.1};
GN   ORFNames=CLOSPI_01624 {ECO:0000313|EMBL:EDS74569.1};
OS   Thomasclavelia spiroformis DSM 1552.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Coprobacillaceae; Thomasclavelia.
OX   NCBI_TaxID=428126 {ECO:0000313|EMBL:EDS74569.1, ECO:0000313|Proteomes:UP000004910};
RN   [1] {ECO:0000313|EMBL:EDS74569.1, ECO:0000313|Proteomes:UP000004910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1552 {ECO:0000313|EMBL:EDS74569.1,
RC   ECO:0000313|Proteomes:UP000004910};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Clostridium spiroforme (DSM 1552).";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDS74569.1, ECO:0000313|Proteomes:UP000004910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1552 {ECO:0000313|EMBL:EDS74569.1,
RC   ECO:0000313|Proteomes:UP000004910};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000256|ARBA:ARBA00002290,
CC       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}.
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:EDS74569.1}.
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DR   EMBL; ABIK02000013; EDS74569.1; -; Genomic_DNA.
DR   RefSeq; WP_004610121.1; NZ_DS562852.1.
DR   AlphaFoldDB; B1C311; -.
DR   STRING; 428126.CLOSPI_01624; -.
DR   GeneID; 67386227; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OrthoDB; 9766019at2; -.
DR   Proteomes; UP000004910; Unassembled WGS sequence.
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; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 3.
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   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   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00332};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, 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:UP000004910};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_00332}.
FT   MOD_RES         174
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   586 AA;  63880 MW;  D809F77647A6000E CRC64;
     MSKIIGIDLG TTNSCMAYME NGKAVIIPNA EGNKTTPSIV AFTNDGKRLV GENAKRQAVT
     NPNNTIASIK REMGTNYRKK INNKEYTPQE ISAMILQKLK IDAEAYLQEK ITEAVITVPA
     YFNDAQRQAT KDAGRIAGLN VKRIINEPTA AALAYGLENS YGQKVMVFDL GGGTFDVSII
     EIGNGVIEVL STSGDNHLGG DDFNDCIAKY IVDEFKRIEG IDLSYDQVAM QRIKEAGEKA
     KIELSTMVTT VVNLPFITNT NSGPKNLEIE ITRAKFNDLT RYLVDRLVLP MQNALNDARL
     TPAELNKIIL VGGSSRIPAV QDKIKEITGK EASKSLNPDE CVALGASIQG GKLSGDVSTT
     GNFDVLLLDV TPLTLSIETV GGVATPLIER NTTIPTSHSQ IFTTSANFQT QVEINVLQGE
     RPLAKDNKSL GKFKLKKIKR AMRGVPQIEV TFDIDANGIV NVSAKDLASG NMQSITIENT
     SNMSDADIER AIREAKQYES QDAITKERLV FKNEAENLVI SIEAALAKNG KQLDKATKSN
     IKNELASFKK LTKKVDYETC DQAKFDEIKS AKINLESLAA TLLSMQ
//
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