ID Q1D5W3_MYXXD Unreviewed; 772 AA.
AC Q1D5W3;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=DnaK family protein {ECO:0000313|EMBL:ABF85909.1};
GN OrderedLocusNames=MXAN_3778 {ECO:0000313|EMBL:ABF85909.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF85909.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF85909.1, ECO:0000313|Proteomes:UP000002402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
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DR EMBL; CP000113; ABF85909.1; -; Genomic_DNA.
DR RefSeq; WP_011553791.1; NC_008095.1.
DR AlphaFoldDB; Q1D5W3; -.
DR STRING; 246197.MXAN_3778; -.
DR EnsemblBacteria; ABF85909; ABF85909; MXAN_3778.
DR GeneID; 41361110; -.
DR KEGG; mxa:MXAN_3778; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_8_0_7; -.
DR OrthoDB; 5483810at2; -.
DR Proteomes; UP000002402; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0035438; F:cyclic-di-GMP binding; IEA:InterPro.
DR Gene3D; 3.30.420.40; -; 2.
DR Gene3D; 2.40.10.220; predicted glycosyltransferase like domains; 1.
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 InterPro; IPR011752; PilV_Myxo-type.
DR InterPro; IPR009875; PilZ_domain.
DR NCBIfam; TIGR02266; gmx_TIGR02266; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00012; HSP70; 1.
DR Pfam; PF07238; PilZ; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000002402}.
FT DOMAIN 29..102
FT /note="PilZ"
FT /evidence="ECO:0000259|Pfam:PF07238"
FT REGION 688..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 772 AA; 81559 MW; F6DE1F280B413ACF CRC64;
MTESNQAAVG LVVKLPFATP EEFLAKYGPN VSRGGIYLRA RAVKPPGTAV TLDLKLAGGE
RIIHAAAVVH YVTGQGGQGV LGMGLRFLNA DAPTRRFLDS LVVTLPHAQS DVPPVPPNVG
PPDYTVTPTE QAPVALASEL YAPAPVPGSA SAEAAAAPPR MISNAALNLS SEDPKRAGVV
IGIDLGTTNS CAAYVRNGKP GVLPSREGHN TVPSIIAVNT RGKLVVGHPA KGQMLTNPRQ
TVYGAKRLVG RPFASPVVEQ LKDRFHYEIA ASENGDAGVK LGEDVYTLQQ ISALILREVR
EVAQNQLGHQ VSRAVVTVPA YYNDNQRQAV REAGKLAGLY IERILNEPTS AALAYGFGRK
LNQRVLVYDL GGGTFDASVL ELNDNVYEVI STGGDTFLGG IDFDSSLVTY LLDEFQKTTG
RAFQGDRVAL QRINDAAERA KCALSERSEV RVHVAFVTMI DSKPCDLDVM LSRQKLVELT
EGLVDRTLQV CEEVLRAKKV TPQDIDEVIL VGGQSRFPLV HEKITKFFGK PPSKGVHPDE
AVALGAALLA HSLGQLEGVV LIDVLPMAIG VGLPGGRFKA VMERNTSLPS TKSYTLATHR
DGQTELELTV FQGDSDKAAD NEYLGTLKLE GLPKLPRGAV QVNVTFEVSN ESLLKVTARE
ASSGREVTST FTTRDTPEAV KARLAQLESE APPAPGPAAA ARSAGHAGAT ATGPAAPVKV
PMATAASASA ARPVLVRPAS SAPVSSIPSV SVAVAPKQKG FMGWLKGLFG RA
//
