ID   A0A246FS87_9PSED        Unreviewed;       565 AA.
AC   A0A246FS87;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Molecular chaperone HscC {ECO:0000313|EMBL:OWP68412.1};
GN   ORFNames=CEC48_28445 {ECO:0000313|EMBL:OWP68412.1};
OS   Pseudomonas sp. K2I15.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=2013577 {ECO:0000313|EMBL:OWP68412.1, ECO:0000313|Proteomes:UP000197956};
RN   [1] {ECO:0000313|EMBL:OWP68412.1, ECO:0000313|Proteomes:UP000197956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K2I15 {ECO:0000313|EMBL:OWP68412.1,
RC   ECO:0000313|Proteomes:UP000197956};
RA   Orellana P., Castillo D., Corsini G.;
RT   "Draft genome sequence of the Chilean Antartic Pseudomonas sp. strain
RT   K2I15.";
RL   Submitted (JUN-2017) 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:OWP68412.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; NIXO01000081; OWP68412.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A246FS87; -.
DR   OrthoDB; 9766019at2; -.
DR   Proteomes; UP000197956; 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   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003322}.
SQ   SEQUENCE   565 AA;  62830 MW;  D2772C44ACBC23D3 CRC64;
     MIVGIDLGTT NSLAAVWRGD TTELVPNALG QFLTPSVVGL DDQGRILVGQ AARERLHTHP
     QLTTSLFKRY MGSATEVRLG DRLFRPEELS ALVLKSLKED IERTYGHTVT EAVISVPAYF
     SDGQRKATRI AGELAGLNIE KLINEPTAAA LAYGLHQRDK ETSFLVFDLG GGTFDVSIIE
     LFDGVMEVRA SAGDNFLGGE DFDTLLLDHF IDSQRNAQGF PPRASVLQPL RREAERVRKA
     LGQDDSAEFS LRVDGQQWAH TITQQELAKL FSPLLERLRT PIERALRDAR IRVGDLDEIL
     LVGGTTRMPL VRKLAAGLFG RFPSISLDPD QVVAHGAAIQ AALKARSAAL EEVVLTDVCP
     YTLGIETSNQ YGNHIESGHY LPLIERNSSV PVSRVKTVHT MHDNQAQVLL KIFQGESRLV
     KDNIKLGELE IEVPKRKAGE VSLDVRFTYD NNGLLEAQVS IPLTGEQHSL VIENNPGVLT
     PAEIQQRLQA LALLKIHPRD QQVNTVLTAR LERLYQESLG ELREQLGHWA AQFQQVLDTQ
     DERRIREART ELTRQLEQLD SGIWR
//