ID A0A0M2SYP9_9BACI Unreviewed; 625 AA.
AC A0A0M2SYP9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=WQ57_12360 {ECO:0000313|EMBL:KKK37745.1};
OS Mesobacillus campisalis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=1408103 {ECO:0000313|EMBL:KKK37745.1, ECO:0000313|Proteomes:UP000034166};
RN [1] {ECO:0000313|EMBL:KKK37745.1, ECO:0000313|Proteomes:UP000034166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA2-6 {ECO:0000313|EMBL:KKK37745.1,
RC ECO:0000313|Proteomes:UP000034166};
RA Mathan Kumar R., Kaur G., Kumar A., Singh N.K., Kaur N., Kumar N.,
RA Mayilraj S.;
RT "Taxonomic description and genome sequence of Bacillus campisalis sp. nov.,
RT a novel member of the genus Bacillus isolated from solar saltern.";
RL Submitted (APR-2015) 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:KKK37745.1}.
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DR EMBL; LAYY01000012; KKK37745.1; -; Genomic_DNA.
DR RefSeq; WP_046524083.1; NZ_LAYY01000012.1.
DR AlphaFoldDB; A0A0M2SYP9; -.
DR PATRIC; fig|1408103.3.peg.2781; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000034166; 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; 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; 2.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
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}; Reference proteome {ECO:0000313|Proteomes:UP000034166};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT REGION 1..341
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 487..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..625
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 625 AA; 72392 MW; F8FC227AB112D7A7 CRC64;
MEKVQFQAES KRLLEMMINS IYSQREVFLR ELISNSSDAI DKIYYKALTD DSLTFNQEDY
YIKVVPDKES RTLKIIDTGI GMTKEELENN LGIIAKSGSL AFKKENELRD GHDIIGQFGV
GFYAAFMVAD VVTVVSKALN SEQAYKWESE GADGYIIVPA DKESVGTEIT LKLKENTEDE
SYDEYLEEYR LKQIIKKYSD FIRYPIKMDV TSSRPKEGTE GDYEQYTEEE TINSMVPIWR
KNKNELTDED YSSFYSEKHY GFDKPLKHIH ISVDGTIRYN AILFIPEKTP FDFYSKEYEK
GLELYSNGVL IMNKCADLLP DYFSFVKGLV DSEDLSLNIS REMLQHDRQL KLIAKNITKK
IKSELQSLLK NERDKYEKFF EAFGRQLKYG VYSDFGANKD TLQDLLLFYS SKEKKLVTLD
EYVSRMPEDQ KYIYYASGES VERIDKLPQA ELVTEKGYEL LYFTDEIDEF AIRMLMTYKE
KEFKSVSSGD LGLDPEEETS DNSEQDENKE LFVAMKELLE GKVKDVRASK RLKSHPVCLS
SDGEITIEME KILQSMPDNQ NIKAEKVLEI NVNHEVFQSL KSAHEKDKDK LSLYTNLLYN
QALLIEGLPI QDPVEFTNDI CKVMV
//
