ID   A0A0N0GQQ9_9NEIS        Unreviewed;       577 AA.
AC   A0A0N0GQQ9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Chaperone protein HscC {ECO:0000313|EMBL:KPC55011.1};
GN   Name=hscC {ECO:0000313|EMBL:KPC55011.1};
GN   ORFNames=WG78_00090 {ECO:0000313|EMBL:KPC55011.1};
OS   Amantichitinum ursilacus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chitinibacteraceae; Amantichitinum.
OX   NCBI_TaxID=857265 {ECO:0000313|EMBL:KPC55011.1, ECO:0000313|Proteomes:UP000037939};
RN   [1] {ECO:0000313|EMBL:KPC55011.1, ECO:0000313|Proteomes:UP000037939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IGB-41 {ECO:0000313|EMBL:KPC55011.1,
RC   ECO:0000313|Proteomes:UP000037939};
RA   Kirstahler P., Guenther M., Grumaz C., Rupp S., Zibek S., Sohn K.;
RT   "Draft genome sequence of the Amantichitinum ursilacus IGB-41, a new
RT   chitin-degrading bacterium.";
RL   Submitted (JUL-2015) 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:KPC55011.1}.
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; LAQT01000001; KPC55011.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0GQQ9; -.
DR   STRING; 857265.WG78_00090; -.
DR   PATRIC; fig|857265.3.peg.19; -.
DR   Proteomes; UP000037939; 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; 2.
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:UP000037939}.
SQ   SEQUENCE   577 AA;  64012 MW;  889005F75D5B4F0C CRC64;
     MRKNLTMLIG IDLGTTNSLC AVWRDGAAQL IPNALGQTLT PSVVGLDDEG RVLVGLPARE
     RLITHPQHTA AVFKRYMGSA HQTTLGTQRF RPEELSALVL QSLKADAERF LGEPVTEAVI
     TVPAYFSDAQ RKATRHAGEL AGLKVASLLN EPTAAALAYG LHQREAESTF LVFDLGGGTF
     DVSILELFDG VMEVRASAGD NFLGGEDFVS VLIEGFVQQH PDLKRLLDPA HRQGDQFRQL
     VRKEAERVKR ALTDQTSVEF SLVWQDHPFS WTVREDDYAR LIDPLLVRLR KPLERALRDS
     RLKLADLDEI VLAGGASRMP LVRRMVARLF GRLPAVHLNP DEIVAMGAAV QAGLKSRDAA
     LREVVMTDVC PYTLGIETSR QYGPGQFQGG LYLPIIERNT VVPVSRSETV YTVRDNQKSV
     LFKIYQGESR EVKDNVFLGE LELDVPPRPA GAVDIEVRFT YTIDGLLETE CVVPESGEKK
     RLLIEKTPGA LSADEVQAQL EKLAALKIHP RAQTENTFLL NRAARLYQET LGHERVVVGE
     ALSQFRAILE TQDERLIEEG RKALHRVLTD LEGEVLL
//