ID L8M396_9CYAN Unreviewed; 538 AA.
AC L8M396;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Molecular chaperone {ECO:0000313|EMBL:ELS03693.1};
GN ORFNames=Xen7305DRAFT_00034170 {ECO:0000313|EMBL:ELS03693.1};
OS Xenococcus sp. PCC 7305.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Xenococcaceae;
OC Xenococcus.
OX NCBI_TaxID=102125 {ECO:0000313|EMBL:ELS03693.1, ECO:0000313|Proteomes:UP000011203};
RN [1] {ECO:0000313|EMBL:ELS03693.1, ECO:0000313|Proteomes:UP000011203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7305 {ECO:0000313|EMBL:ELS03693.1,
RC ECO:0000313|Proteomes:UP000011203};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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:ELS03693.1}.
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DR EMBL; ALVZ01000155; ELS03693.1; -; Genomic_DNA.
DR RefSeq; WP_006509231.1; NZ_ALVZ01000155.1.
DR AlphaFoldDB; L8M396; -.
DR STRING; 102125.Xen7305DRAFT_00034170; -.
DR PATRIC; fig|102125.3.peg.2037; -.
DR eggNOG; COG0443; Bacteria.
DR OrthoDB; 416657at2; -.
DR Proteomes; UP000011203; 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; cd10170; HSP70_NBD; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF513; SLR0086 PROTEIN; 1.
DR Pfam; PF00012; HSP70; 2.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
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:UP000011203}.
SQ SEQUENCE 538 AA; 59979 MW; 3B441BE8C7A8F0FC CRC64;
MADNLNSTNS YAIDFGTSNT VITRWNGVTK TAETITFPNF SQKIPNSPPV IPSLVYVKDA
RLQKVLIGQQ VRDRGLDLAT DNRFFRSFKR GIGADIQGFL PRLDETEITF EQIGEWFLRE
LIQNSQTDAG GNLDSLVVTV PVDSFDTYRL WLTDICQSLE IGQLRILDEP TAAALGYGAA
DQELLLVVDF GGGTLDISLI QLSENTSSNQ GFILKWGQKI LGENTAQKKQ TAKVIAKAGQ
NLGGSDIDNW LVDYFATNQG LDKSAVTTRL AERLKIKLSE QESATEVYFN DETLESYALE
LDRQGFEAIL EQQGFFTKLD ELMAQVLQRA RRNGIEVEEI NQVLLVGGTV QIPAVQTWVA
KYFEPSKIRC DRPLTAIAEG ALQVAQGIEV KDFLYHSYGI RYWNRRDKRH NWHSIIKSGQ
PYPMAQPVRL VLGASVENQP SIELILGELA TESVGREVYF DGDRLVTRSL GEQTTNVKPL
NDQEGASTIA ILDPPGNPGR DRIELLFSVD EQSCLRVTVQ DLLTQETLLD NQIVGQLK
//
