ID A0A1G0XJJ5_9BACT Unreviewed; 1182 AA.
AC A0A1G0XJJ5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A2523_06510 {ECO:0000313|EMBL:OGV33860.1};
OS Ignavibacteria bacterium RIFOXYD12_FULL_36_8.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798454 {ECO:0000313|EMBL:OGV33860.1, ECO:0000313|Proteomes:UP000177243};
RN [1] {ECO:0000313|EMBL:OGV33860.1, ECO:0000313|Proteomes:UP000177243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGV33860.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MHBA01000020; OGV33860.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0XJJ5; -.
DR STRING; 1798454.A2523_06510; -.
DR Proteomes; UP000177243; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 268..320
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 534..753
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 776..889
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 898..1014
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1060..1176
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 469..524
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 825
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 947
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1109
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1182 AA; 133781 MW; 0DC177EE235D250C CRC64;
MKISYRILFI NFFVVVLIIG SASFAFYSIM YNVLTSQQSK YLLKSSNDFI FAYNETFQNT
EDDFNQLSRT ELFSGERLKS TSIDFILEQD SKNVKIYSRS VVKAGVNLSQ KFSSLEEFIS
NNPSAVIKSH TFPDGTSVYY GRLLTDEFLN SIAQKINAQV VIITGNSTLQ VSNQSANQQY
IYFLNKAYNN LSRREKFNVY SEDSGQADII STLCNISSNI NENQNLKFLI FSTLNEAADL
RSSIKYILIT VGIAGVLLSL ILTFMFTQKI RSQLHLLSNA TELTKQGNFK NKIEIKSNDE
IGQLASAFNN MLDELDKHDR AITDYSDFIA LINRNASLKE IADAALNKII KTCGFAVGAI
YAVKGSSITL IRSYGIKGKT AAEDYEFFDS AIKNREMLEL NFEKNFPTVS SGIISLEIKH
MLLIPIIYNN EVIALLELGG LDSPSQAVKN YLSKIQEQLA IGLTNAFAFV QLENLVVELK
LLNEEYQKQN QQVKQQNESL IKLHDQLRDK ARELEVQKLR AEESTKLKSQ FLASMSHELR
TPMNSVLGLT ELILDESTLL NPKTKERLEI VHRSGKRLMS LINDILDLSK IEAGKMDLKH
DDVLLEDIIL DLEASIRPLV VKKHLELKIV RKANTNVFIA TDRGKVTQVL INLLGNAIKF
TERGFVELHV DDLGENQLRF DVVDSGIGIS IEDQKIIFEE FRQIDGTAAR KYSGTGLGLS
ICKKIAEMLN GSLSVESQLN KGSVFSFIIP FKVSSEKERQ KQSVNVETLR KNRKNPILVI
DDDADIRITI GQYLESRGYK VVYADNGASG VNLAKELQPF AITLDLLLPN KDGWTVLKEL
KENPATKNIP VILVSIIGDK NLGYGLGAFE YFVKPISHNE LLSAFNKLEN YARKKIEKII
LVDDDELEFE RFKRVLHNDG VTVHFIKDSQ FAFNKIVDIQ PDLIVLDLLM PGIDGITLTH
ELRNYKETKH IPIIISTAKD LNDEEKNSLR HIVEDITVKS KGHPHDVLKI VRDRIRMDEL
SYYVEDTAGK QPLEEIEILS DQIRNVSLDE KKNRKELLGE VLIVDDDPDT LFTINEIVQS
CNCTTFVAKN GLECLNILEK NLPDLILLDI MMPEMDGFQT IKKIRENSNW RHVPVFAVTA
RAMLEDRQII LKNGFDDYIT KPVNAGVISF KIEKLFSKIR AT
//
