ID A0A2B8BMZ2_9PROT Unreviewed; 940 AA.
AC A0A2B8BMZ2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CRT60_05505 {ECO:0000313|EMBL:PGH58597.1};
OS Azospirillum palustre.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=2044885 {ECO:0000313|EMBL:PGH58597.1, ECO:0000313|Proteomes:UP000225379};
RN [1] {ECO:0000313|Proteomes:UP000225379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B2 {ECO:0000313|Proteomes:UP000225379};
RA Kravchenko I.K., Grouzdev D.S.;
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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};
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:PGH58597.1}.
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DR EMBL; PDKW01000038; PGH58597.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B8BMZ2; -.
DR OrthoDB; 9796100at2; -.
DR Proteomes; UP000225379; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 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; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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 PANTHER; PTHR43065:SF49; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PGH58597.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 462..517
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 555..776
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 797..907
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 13..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 505..532
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 846
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 940 AA; 101612 MW; CF586EA5739476D0 CRC64;
MMADPVWQDA ARLRQSAGPV RAAGGMENPD GMKSRAGSGP DVFTGGGEMG RRMREMDWSA
TPLGPPEHWP QSLRTTVNLM LTSGFPMFTA WGPELTFLHN DSYRPILGDK PEALGRPFAE
VWAETWHQLI PLVARALSGE AFYHQDLQLF MERHGYWEET YFTFSYSPVR DEAGHVAGMF
CACTENTARV LAERRLTFQL DLAEKLRGLN DPVGITAAAA EAIGRHLRVA RAGYGRIDPT
GSMISVDRDW SDSGVESLAG QSRPLDSFGP ALIAELRAGY TLRVDDVATD PRTSGSGPAA
GFAGIGARAL LVVPLLKAGQ LTAILYLHES EARHWTETDA ALAEDVAERT WAAVERALAE
AALRAANTAL IRERAAVEAA NARLAAEGER LRTLFRQAPS FMCVLRGPDH VFELANDTYM
QLVGRQDLVD RPARDALPEV EGQGFFELLD RVYASGETFV GHSMPISFRR RPDGPLEERF
LTFVYQPIKD EDGRVTGLFV EGSDVTEAKR AEEELQQLNA TLEARVAEEV AERERVQIAL
LQTQKTEALG QMTGGVAHDF NNLLQALSGC LHMIEKRAEG TRIQPLVDAG RQAVDRGAKL
VQQLMAFARR QALRPETVDL RDRVLGMSEL LNRALRADIR LEVDFAAGLW PVEVDATQLE
LALLNLVVNA RDAMPDGGML SIRAANVTLT HGDPQAPNGL SGEFVRLTVS DTGTGMPADV
QARAFDPFFT TKEIGKGSGL GLSQVYGFAR HSGGTVWIES EEGRGTTVGL LIRRSGTAPA
TAAEPVAEAG ASRVGGHVLV VEDDPIVALT VATALEDAGF TVTRAATADE ALPLLEAGGF
DLLFSDVVMP GTMSGVDLAR SAQRLRPDLP VVLATGYSEE VARATGVMVL AKPYRIDHLV
EVLDTLLTEA KRVEGEAPSP VPGEGMEPTA TGRTSAEGRS
//
