ID   A0A2N7VFC1_9BURK        Unreviewed;       574 AA.
AC   A0A2N7VFC1;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Molecular chaperone HscC {ECO:0000313|EMBL:PMS15814.1};
GN   ORFNames=C0Z18_25375 {ECO:0000313|EMBL:PMS15814.1};
OS   Trinickia dabaoshanensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Trinickia.
OX   NCBI_TaxID=564714 {ECO:0000313|EMBL:PMS15814.1, ECO:0000313|Proteomes:UP000235616};
RN   [1] {ECO:0000313|EMBL:PMS15814.1, ECO:0000313|Proteomes:UP000235616}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GIMN1.004 {ECO:0000313|EMBL:PMS15814.1,
RC   ECO:0000313|Proteomes:UP000235616};
RA   Estrada-de los Santos P., Palmer M., Chavez-Ramirez B., Beukes C.,
RA   Steenkamp E.T., Hirsch A.M., Manyaka P., Maluk M., Lafos M., Crook M.,
RA   Gross E., Simon M.F., Bueno dos Reis Junior F., Poole P.S., Venter S.N.,
RA   James E.K.;
RT   "Whole genome analyses suggest that Burkholderia sensu lato contains two
RT   further novel genera in the rhizoxinica-symbiotica group Mycetohabitans
RT   gen. nov., and Trinickia gen. nov.: implications for the evolution of
RT   diazotrophy and nodulation in the Burkholderiaceae.";
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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:PMS15814.1}.
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DR   EMBL; PNYA01000028; PMS15814.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N7VFC1; -.
DR   OrthoDB; 9766019at2; -.
DR   Proteomes; UP000235616; 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; cd10235; HscC_like_NBD; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR042030; HscC_NBD.
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; 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.
DR   PROSITE; PS01036; HSP70_3; 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:UP000235616}.
SQ   SEQUENCE   574 AA;  63188 MW;  3C75BC9BF8E65DBD CRC64;
     MIVGIDLGTT NSLIAIWQDG QPRLIPNSLG EYLTPSCVSI DEDGSILVGR AARERLQTHP
     DKTAAVFKRF MGSERVIRLG RREFRAEELS ALVLRSLKED AETALGQPVT EAIITVPAYF
     SDAQRKATRT AGVLAGLKVD RLLNEPTAAA LAYGIHQLGA ETRFLVFDLG GGTFDVSVLE
     MFEGVMEARA SAGDNFLGGE DFVACLIDRF FELTKAPARL KTDAGFMQRL TAGAEAAKRT
     LTEQSAATIE MVGVGETYTM QIDEEAFEQA CAPLLQRLRS PVERALRDAN LRDTDLEKVV
     LAGGATRMPI VRRLVARMFG RFPECQIDPD QVVALGAAVQ AGLKMKDAAL DEVVMTDVAP
     YSLGVGVAMQ LPDGSQSGGH FDPIIERNSP VPISRVKTYH PVRDHQLTVD LHVYQGEARL
     VADNILLGSL KIPLPRLPRA ECGVDVRFTY DVNGLLDVEA TIQKTRETTR VLIEGNPGLL
     SEAEITERLT ALAALKIHPR DRMENRVLMA RAERLYQQLR GSEREWFGAQ IRVFESALAS
     QDSRRIDADR RTFDEIVNGV ERANRIFPLP EPQN
//