ID G2IZ96_PSEUL Unreviewed; 854 AA.
AC G2IZ96;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=NH8B_3452 {ECO:0000313|EMBL:BAK78205.1};
OS Pseudogulbenkiania sp. (strain NH8B).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Pseudogulbenkiania.
OX NCBI_TaxID=748280 {ECO:0000313|EMBL:BAK78205.1, ECO:0000313|Proteomes:UP000001274};
RN [1] {ECO:0000313|Proteomes:UP000001274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NH8B {ECO:0000313|Proteomes:UP000001274};
RX PubMed=22038961; DOI=10.1128/JB.06127-11;
RA Ishii S., Tago T., Nishizawa T., Oshima K., Hattori M., Senoo K.;
RT "Complete genome sequence of the denitrifying and N(2)O-reducing bacterium
RT Pseudogulbenkiania sp. strain NH8B.";
RL J. Bacteriol. 193:6395-6396(2011).
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; AP012224; BAK78205.1; -; Genomic_DNA.
DR AlphaFoldDB; G2IZ96; -.
DR STRING; 748280.NH8B_3452; -.
DR KEGG; pse:NH8B_3452; -.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR HOGENOM; CLU_000445_114_75_4; -.
DR Proteomes; UP000001274; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00130; PAS; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; IPR011006; CheY-like_superfamily.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; NF041832; near_NosP_CTERM; 1.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF9; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF12860; PAS_7; 2.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 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; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:BAK78205.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000001274};
KW Transferase {ECO:0000313|EMBL:BAK78205.1}.
FT DOMAIN 325..395
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 397..449
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 492..705
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 732..849
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 11..97
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 437..485
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 783
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 854 AA; 94186 MW; 265A3923EC13DFB4 CRC64;
MAPRSNGAER LYALELENAK LRKINEALMR RVEQGLADNG NSFTFFQVAA ELETRIQERT
RALEKAMADL EASNFALQEA KLAAELAKNQ LNVAVETIAD GFALWDSDNR LIHCNRKFGE
MFPALRPIIA PGLPFETLIR AAVAAHLIRD AEADPEDWIA QRLAVQQAPQ DSLILAMSDG
SWQRVSERAI AGGGRVAIYT DITEIKRQEM LLRERDLAAH SQLLHATMNS IRQGLAVFDR
DGRLMEWNPR FVELTQPALA QLDEGGGVHL AEWSRCCPLG GTLEYRTPQG LTLEVQYNPM
QGGGFVMSYT DISERKAAEQ ALRDSEAKMR LITDAMPALI AYVDNQQIYR FTNKGYESWF
GVPQSEINGR SMREVLGAQL FDDRKHFVEL ALSGQASVFE LELPAPRQHI EFARATFIPH
FASDGSVLGF FALIQDITES RRAAEALQQA KEQLEVRVAE RTEELSVANG RLREAIRAIE
DAQQSKTRFF AAASHDLLQP LNAARLFLAA LAGQELAPPV RPLVDKTGTA LESVDDLINT
LLEISRLDAG AVEAEPRHFP VAQLLEQVAE EFAPLAEAKS LRLQLHSSPA IIHSDWVLLG
RVLRNFLSNA IRYTREGGIL LGCRRQPDGL LIGVWDQGLG IPSDKLALVF HEFQRLPEHH
SLCPKGMGLG LAIVSRLARR LDHRLVVRSR FGRGSLFGVV VPYGEADAVG PAPQPEDPLP
ALAAPAQRQG ATILLIDNET SILEGMSTLL ADWRYRPLAA ASASEAIELL KREAVQPDAI
LADYHLDHGA TGIEAIRAVC QHLGRAVPAA LITADRSDEV RQEAEAGGWA WLGKPVRPAR
LRTLLAHLTQ PAGE
//
