ID F2K2P5_MARM1 Unreviewed; 642 AA.
AC F2K2P5;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 OrderedLocusNames=Marme_1929 {ECO:0000313|EMBL:ADZ91178.1};
OS Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 /
OS MMB-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=717774 {ECO:0000313|EMBL:ADZ91178.1, ECO:0000313|Proteomes:UP000001062};
RN [1] {ECO:0000313|EMBL:ADZ91178.1, ECO:0000313|Proteomes:UP000001062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1
RC {ECO:0000313|Proteomes:UP000001062};
RX PubMed=22675599; DOI=10.4056/sigs.2545743;
RA Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA Detter J.C., Copeland A., Teshima H., Bruce D., Detter C., Tapia R.,
RA Han S., Land M.L., Ivanova N., Mikhailova N., Johnston A.W.,
RA Sanchez-Amat A.;
RT "Complete genome sequence of the melanogenic marine bacterium Marinomonas
RT mediterranea type strain (MMB-1(T)).";
RL Stand. Genomic Sci. 6:63-73(2012).
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}.
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DR EMBL; CP002583; ADZ91178.1; -; Genomic_DNA.
DR RefSeq; WP_013661083.1; NZ_CP047696.1.
DR AlphaFoldDB; F2K2P5; -.
DR STRING; 717774.Marme_1929; -.
DR KEGG; mme:Marme_1929; -.
DR PATRIC; fig|717774.3.peg.1989; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_6; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000001062; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000001062};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 30..187
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..350
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 568..642
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 642 AA; 73045 MW; 49541CEA3C3DE39A CRC64;
MATETQKETL GFQTEVKQLL HLMIHSLYSN KEIFLRELIS NASDAVDKLR FESVSNADLL
SEDPNLRVRL EFDNEAGTVI IDDNGIGMNR DDAINNLGTI AKSGTAQFLE QLSGDQKKDS
QLIGQFGVGF YSAFIVADKV TVETRKAGAA TDEAVRWESS GDGDFTIEAI EKETRGTRIT
LHLKADEKDF ADNYRLRSLV TKYSDHISIP VEMEKVVYPE MDEEGNPKPV DENQAVEFEA
VNSAKALWTR ARSEVSDEEY SEFYKHVSHD FQDPIKWSHN KVEGKLEYTS LLYVPSKAPH
DLWNRDMQRG LKLYVQRVFI MDEAEAFLPP YMRFVKGVVD SNDLSLNVSR EILQNDKAVD
SMRSALTKRV LDMLSKMAKN ESEKYQTFWD EFGNVLKEGP ADDFGNKDKI AQLLRFSTTH
TDKAEQTESL AGYVERMSEG QDKIYYIYAE NHNTAKNSPH LEILRKKGFE VLLLSDRIDE
WMMSSLQEFD GKKFQDVTKG KLDLAEDETE EAKKEKEQKA EEIKPLLDRM KAVLEEQVTD
VTSTDRLTNS PACLVVGEYD MGLQMRRLLE QAGQAMPESK PSLEINPDHP IVVKMDSEAD
EERFSDMAWL LFEQATLSEG GQLDDPASFV SRMNKLIVQL SQ
//
