ID D2R9I9_PIRSD Unreviewed; 753 AA.
AC D2R9I9;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Psta_3075 {ECO:0000313|EMBL:ADB17739.1};
OS Pirellula staleyi (strain ATCC 27377 / DSM 6068 / ICPB 4128) (Pirella
OS staleyi).
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Pirellula.
OX NCBI_TaxID=530564 {ECO:0000313|EMBL:ADB17739.1, ECO:0000313|Proteomes:UP000001887};
RN [1] {ECO:0000313|EMBL:ADB17739.1, ECO:0000313|Proteomes:UP000001887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27377 / DSM 6068 / ICPB 4128
RC {ECO:0000313|Proteomes:UP000001887};
RX PubMed=21304671; DOI=10.4056/sigs.51657;
RA Clum A., Tindall B.J., Sikorski J., Ivanova N., Mavrommatis K., Lucas S.,
RA Glavina del Rio T., Nolan M., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA Goodwin L., Ovchinikova G., Pati A., Mikhailova N., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Pirellula staleyi type strain (ATCC 27377).";
RL Stand. Genomic Sci. 1:308-316(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR EMBL; CP001848; ADB17739.1; -; Genomic_DNA.
DR AlphaFoldDB; D2R9I9; -.
DR STRING; 530564.Psta_3075; -.
DR KEGG; psl:Psta_3075; -.
DR eggNOG; COG3829; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_39_0; -.
DR Proteomes; UP000001887; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065:SF23; SENSOR HISTIDINE KINASE PDTAS-RELATED; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ADB17739.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001887};
KW Transferase {ECO:0000313|EMBL:ADB17739.1}.
FT DOMAIN 134..204
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 205..259
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 260..308
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 461..513
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 533..749
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 753 AA; 84732 MW; 34E59341B4CF74B6 CRC64;
MDLDSFSVND STAHRALLAT GTGIWKWCLV ERCEHWHASL RKALEPCFSI PISDTPSLFS
LLHPRSAQLL RDSLTQIERN DESIDLTLDL ECSASHGTQL RLQAGIDPQD RRQVWAVCHV
AKNSVGAELE RDTSLDVFAS IIDCAVDAII SKSVDGTIRT WNTGAEHLFG YRAEEVIGKP
ITLLIPPDRL NEEEDILRRI WRGERVLNFE SIRRRKDGTD VNVSLTISPI KNQAGVIIGA
SKVVRNITEQ VKTEAKLRES EERFRILFES SPTAILLSND RAEYIDANPA YEQISGYTAE
ELYGKTAIDL GTLPPDSDFQ THAMEQLNAT GRLDNIEVTG PTKYGNLITV LFSTREIEVA
GRREFLTVLL DISERVRAEA ALRKSEERLA EAQRIAHLGD WSWNTLTDEI HWSDEVYRIF
GHEPKSFTPR FRHEFIQAVH AEDQTRVASA MFESLENKER FSIEHRIHQV DGTERFVRLV
GQVTQDPAES AFVLLGTIQD ITDLKNAEQQ AMVLRNQVAH AGRIATMGEM AAGIAHELNQ
PLSAIELYAE GCQRALEMGV LSTEEQLSKL VEIASLADRC GEIIRRLRLF AMNRDSNWSP
IDLTEVVKAS IEFMGYELQK SQTRCVVQIS EEPLLVSADS IELQQVFLNL IKNAIESQEL
SNPKDRRIEI IVKASTDKRI SVIIRDNGCG MQPHQLARIF NPFYTTKSAG LGMGLKICQT
IIRSLRGEIV CQSEPGVGTT FEIVLPVVRR RMK
//
