ID A0A1B8PHT6_MORNO Unreviewed; 640 AA.
AC A0A1B8PHT6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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 ORFNames=A9Z60_04680 {ECO:0000313|EMBL:OBX48688.1};
OS Moraxella nonliquefaciens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=478 {ECO:0000313|EMBL:OBX48688.1, ECO:0000313|Proteomes:UP000092671};
RN [1] {ECO:0000313|EMBL:OBX48688.1, ECO:0000313|Proteomes:UP000092671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 60284 {ECO:0000313|EMBL:OBX48688.1,
RC ECO:0000313|Proteomes:UP000092671};
RA Salva-Serra F., Engstrom-Jakobsson H., Thorell K., Gonzales-Siles L.,
RA Karlsson R., Boulund F., Engstrand L., Kristiansson E., Moore E.;
RT "Draft genome of Moraxella nonliquefaciens CCUG 60284.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OBX48688.1}.
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DR EMBL; LZDN01000043; OBX48688.1; -; Genomic_DNA.
DR RefSeq; WP_066886623.1; NZ_LZDN01000043.1.
DR AlphaFoldDB; A0A1B8PHT6; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000092671; 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 Gene3D; 1.20.1270.10; -; 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; IPR029048; HSP70_C_sf.
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; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
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:UP000092671};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 601..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 640 AA; 68508 MW; 8D2650083CBDA32F CRC64;
MGKVIGIDLG TTNSCVAILE NGNVKVIENS EGARTTPSIV AFKDGETLVG QSAKRQAVTN
PQNTLFAVKR LIGRRYDEQA VQKDIGLVPY KIVKADNGDA WVEVNGKKQA PPQISAEVLK
KMKKTAEDYL GETVTEAVVT VPAYFNDAQR QATKDAGRIA GLDVKRIINE PTAAALAFGL
DKKEGDRTIA VYDLGGGTFD VSIIEIADVD GEQQFEVLST NGDTFLGGED FDIALIDHLA
DEFKKEQNVN LKGDPLAMQR LKEAAEKAKI ELSSSTSTEV NLPYITADAT GPKHLVVTIS
RAKLEALTEE LVARTIAPCK TALEDAGLSA SDIDDVILVG GQSRMPLVQQ KVQEFFGKEP
RKDVNPDEAV AIGAAIQGAV LSGDKKDVLL LDVTPLTLGI ETMGGVMTAI IEKNTMIPTK
KSQVFSTAAD NQPAVSIQVY QGERKIASQN KLLGNFDLTD IPPAPRGVPQ IEVTFDINAD
GIMNISAKDK GTGKSQSIQI KADSGLTDEE IEQMVRDAEA NAEADKKFAE LANVRNEADG
RIAGVQKALK ENGDKATDEE KQAVETAISE LELATKEDDV DAIKAKLEAL DNAFLPIGTK
IYSTDQGGAD AGQAPKQDQT KPADDGVVDA EFTEVKDDKQ
//