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Database: UniProt
Entry: A0A1H1MZZ1_9BACT
LinkDB: A0A1H1MZZ1_9BACT
Original site: A0A1H1MZZ1_9BACT 
ID   A0A1H1MZZ1_9BACT        Unreviewed;       896 AA.
AC   A0A1H1MZZ1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN05444173_1339 {ECO:0000313|EMBL:SDR92252.1};
OS   Opitutus sp. GAS368.
OC   Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae; Opitutus.
OX   NCBI_TaxID=1882749 {ECO:0000313|EMBL:SDR92252.1, ECO:0000313|Proteomes:UP000199432};
RN   [1] {ECO:0000313|EMBL:SDR92252.1, ECO:0000313|Proteomes:UP000199432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GAS368 {ECO:0000313|EMBL:SDR92252.1,
RC   ECO:0000313|Proteomes:UP000199432};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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};
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DR   EMBL; LT629735; SDR92252.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1MZZ1; -.
DR   STRING; 1882749.SAMN05444173_1339; -.
DR   Proteomes; UP000199432; Chromosome i.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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; 2.
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; IPR001610; PAC.
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; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
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); 2.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000199432};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        41..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          268..338
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          342..394
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          532..757
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          778..894
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         829
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   896 AA;  98300 MW;  A91BB5CC87413C79 CRC64;
     MSGWFTQNTD YLVFLVLVAS LWLGLGLWLH RTGRLASLPK ITWLLLAVVA GGGWWAVNRA
     GYDAQGNIRR QVELLVPYYV QEMQQAGHAR LADNPPPGDA LYEKLIQMEI NWLKLNPAIA
     DVYTFRRRAD GAIFLLADSE TDYDHNGRIA SARGQRTPPG EIYEGLTPAL NRAFRGELIF
     DEDIVEDRRG RWVSVFAPLR NASGLVEAVL GVDFDATQWL EQRTRARLMT LWFLGGAILL
     FTGPALLVTV LRHDLQRRRQ VEVQLREQAE VRRIIFDHAP GGIALADLNN RLLEVNDALC
     TMLGYRRDEL LQLSFVQITH PDDVGKNLTL NRQITSGEIR VGQLEKRYIR KDGSVIHAAL
     SVGLARDEQG APRFFVGQVT DITERRQVES ELHLRQKQLA AILAHAPIIL FATDLQGIYT
     LCEGAALTAI GYQPGAAVGQ SIFDRYAARP DILGDIRRAL AGESLAIQRE INGVIFEGRC
     MPQREADGRI TGMIGITIDV TDRVAAARER EKIEHKLLEV QKLESLGVLA GGVAHDFNNL
     LTAIMGNTSL ARQSLPPGSP LTGNLDQVEQ ASQLAAGLCQ QLLAYAGRSR LDPQITDLNT
     LVRETTDLLR LSIGNHAQLR LNLAPDLPGL MADPAQIRQV LLNIVQNAAE AIGRRDGVIT
     LTTRVLAVDA AWLAEASSGR ELPPAAYVCL EVTDNGPGLD RAARSRVFDP FFSTKGSGRG
     LGLAAALGIM RSHKGALRLV SEPGQGATFT LAFPPNARPA PKSVASAPSA PTWRSSGTVL
     IVDDEQAVRA TAAQMIAFFG FTVKQAESGQ QALDFLRQRG SRFDLVLLDL TMPGMDGYAT
     FTALRQLQPD QRIVVFSGYS AQDAQQRFAG QNLNGFLQKP FSTDSLRDVL REATLN
//
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