ID Q2C5B7_9GAMM Unreviewed; 633 AA.
AC Q2C5B7;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 24-JAN-2024, entry version 90.
DE RecName: Full=Chaperone protein HtpG {ECO:0000256|HAMAP-Rule:MF_00505};
DE AltName: Full=Heat shock protein HtpG {ECO:0000256|HAMAP-Rule:MF_00505};
DE AltName: Full=High temperature protein G {ECO:0000256|HAMAP-Rule:MF_00505};
GN Name=htpG {ECO:0000256|HAMAP-Rule:MF_00505};
GN ORFNames=SKA34_02574 {ECO:0000313|EMBL:EAR56234.1};
OS Photobacterium sp. SKA34.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=121723 {ECO:0000313|EMBL:EAR56234.1, ECO:0000313|Proteomes:UP000005284};
RN [1] {ECO:0000313|EMBL:EAR56234.1, ECO:0000313|Proteomes:UP000005284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKA34 {ECO:0000313|EMBL:EAR56234.1,
RC ECO:0000313|Proteomes:UP000005284};
RA Hagstrom A.J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Molecular chaperone. Has ATPase activity. {ECO:0000256|HAMAP-
CC Rule:MF_00505}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00505}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239, ECO:0000256|HAMAP-Rule:MF_00505}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00505}.
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:EAR56234.1}.
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DR EMBL; AAOU01000010; EAR56234.1; -; Genomic_DNA.
DR RefSeq; WP_006646850.1; NZ_CH724144.1.
DR AlphaFoldDB; Q2C5B7; -.
DR HOGENOM; CLU_006684_3_0_6; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000005284; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR CDD; cd16927; HATPase_Hsp90-like; 1.
DR Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.40.50.11260; -; 1.
DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR PANTHER; PTHR11528:SF97; ENDOPLASMIN; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00505};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00505};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00505};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505,
KW ECO:0000313|EMBL:EAR56234.1}.
FT DOMAIN 33..190
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..344
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 562..633
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 633 AA; 72140 MW; 82B18934685645D9 CRC64;
MSNQVVDKNK ETRGFQSEVK QLLHLMIHSL YSNKEIFLRE LISNASDAAD RLRFKALSQS
DLYGDDSNLC VKLSINEQAG TLTISDNGIG MTREQAIEHL GTIAKSGTKE FFSQLKEDES
KDSQLIGQFG VGFYSAFIVA DSVTVNTRAA DAAVDEAVSW QSAGEGDYSI ETITKANRGT
DIILHLREDD KEFLNEYRLR EIVGKYSDHI GIPVLIQTEE KDEEGKVTGT KWDQINKAQA
LWTRNKSDIS EEEYKEFYNH VAHDYAEPLV WSHNRVEGKQ DYTSLLYIPS TAPWDLNNRD
GQHGLKLYVQ RVFIMDDAQQ FMPTYLRFVR GLIDSNDLPL NVSREILQDN KVTQALRKAC
TKRVLQMLER MAKNDAEKYQ TFWKAFGQVL KEGLAEDSAN REKIANLLRF SSTESDSQEQ
RVSLADYVSR MKENQDKIFY LTADNFNAAK HSPHLEQFRA KGLEVILMYD RIDEYLMGHL
PEFEGKQFQA ITKSDLDLSS FDDEEVKEKQ KEAEKEFASV TERTKGYLGS RVKDVRATFK
LHDTPAVVVT DENEMGTQMA KLLAAAGHDA PEVQYIFELN PEHALVKKMA DEVDEEVFGR
WVEFLLGEAM LAERGTMEDP SQFLAAINKL LIK
//
