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Database: UniProt
Entry: A0A0M2UTU1_9BACT
LinkDB: A0A0M2UTU1_9BACT
Original site: A0A0M2UTU1_9BACT 
ID   A0A0M2UTU1_9BACT        Unreviewed;      1395 AA.
AC   A0A0M2UTU1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BROFUL_01822 {ECO:0000313|EMBL:KKO19483.1};
OS   Candidatus Brocadia fulgida.
OC   Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC   Candidatus Brocadiaceae; Brocadia.
OX   NCBI_TaxID=380242 {ECO:0000313|EMBL:KKO19483.1, ECO:0000313|Proteomes:UP000034954};
RN   [1] {ECO:0000313|EMBL:KKO19483.1, ECO:0000313|Proteomes:UP000034954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RU1 {ECO:0000313|EMBL:KKO19483.1};
RX   PubMed=24267221; DOI=10.1186/1471-2180-13-265;
RA   Ferousi C., Speth D.R., Reimann J., Op den Camp H.J., Allen J.W.,
RA   Keltjens J.T., Jetten M.S.;
RT   "Identification of the type II cytochrome c maturation pathway in anammox
RT   bacteria by comparative genomics.";
RL   BMC Microbiol. 13:265-265(2013).
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:KKO19483.1}.
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DR   EMBL; LAQJ01000189; KKO19483.1; -; Genomic_DNA.
DR   PATRIC; fig|380242.3.peg.2266; -.
DR   Proteomes; UP000034954; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 4.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 2.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 4.
DR   InterPro; IPR003018; GAF.
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; 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; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 4.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 2.
DR   Pfam; PF08448; PAS_4; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 2.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 4.
DR   SMART; SM00091; PAS; 4.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 2.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 3.
DR   PROSITE; PS50112; PAS; 4.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KKO19483.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034954};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        190..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          215..267
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          498..568
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          554..619
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          620..689
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          691..743
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          744..801
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          1037..1115
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          1108..1161
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          1174..1395
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   1395 AA;  158433 MW;  AB52F0895D39EA8D CRC64;
     MIGIRAKLML FMSTLVIIIS TLSCVFFLIH AKRQQEETLK NFGMSLVMLL AQDHEVKYAM
     TYTQPAFLDA PVKRIRALDR EEEIGYLRIS NVQTTLMEEK TPWMGIDMKE IPIQKGRENQ
     EILYSNCMLA CSQKAFYDFS LAVTEEKTFS EEAFAAQVLE EITMKAGQHP LGFIQIGLSS
     HKLGKRIHRI FWKSVIPLGL IIISGGISTI IFLTKYLVSP LRQMANVTLD IAKGDLTRTV
     DVQSYDEIGQ LSVNFNKMTR SLKKSYDDLK QEIVERRRAE GLLGFRVKIE ELIAAISTNF
     INLPPSEVDA GIDRALQQIG EFSDVDRSYV FLNTPDGKKI DNTHEWCAKG ILPQKENLQG
     VFVEQFPWGM EKLRRFETLH IPRINDLPED AKAERALQQS QEVQSCVIVP MIYGGSLMGL
     LGFDSVRREK TWTQEDIAML KMVAEIFVNA LEHKRMEEAL RKANSELELR VEERTLELSK
     TNAILKEEIV EHKKARDALR KYEILISEMT DLAYICDTEG NIVFVNPTFE KLTSHPPEEF
     IGKSFAPLFD DENYKKGMRF YTNTLEGESP RFEIYFKDTG VLCEYNNMPL RDDQGNIIGV
     IGIARDITER KRMENILRET NQTLQAIILA SPLAITVLDS RGCVKIWNPS AERIFGWKEQ
     EVLGHGLPIV SSDKQHEFIG LRDQVLRGES FMVELWRRRK DGSLINISLS TAPLYGHHGN
     VEGILGIMSD NTERQKMMND LQQAKDYAEN LIETANIMVV ELDVMGNIQI FNKVAEEITG
     YKKEEIIGRN WFEVIVPRER NPYVWEEFSL WQSGGPLPKT MEAPVFTKLG KKRYVSWQNS
     EVREQGKTIG TISFGVDITE QKRNKELVER IRLMAFLKDI GIALTASEPL REMLSQCTDA
     VVSNLDVAFT RIWTFNEKEN ILELQASSGR YTHIDGAHGR IPLGKYKIGI IARDRQPHLI
     NSVINDPHIS DKEWVQREGI VAFAGYPLIV KDRLVGVIAM FAQKTITEFA YRAFVSAGDI
     IALGIDRKQA EEALRASERK YRMLLENLPQ RVFYKDENLR YVSCNENYAR DLKISPDEIA
     GKTDYDFYPE ALAEKYRSDD KRIMMLETTE DIEEKYIRDG QEFTIHTVKT PIKDEKGKVI
     GVLGIFWDIT EKIALQMEAI RSRHLASIGE LAATVAHEIN NPITGIINCA QILVNKSEKG
     SKGEDMGIRI VKEGKRIADI VKSLLSLARP GDRKEQKGAV CVSDIVSDTL ALVDSQLKKD
     CIVLVLNLPH TLPRIRAHHQ QIQQVFLNVI SNARYALNAK YPGRHENKML GIRGEAVTMD
     HGRWVKITFH DTGAGIPSDI LDKVMNPFFS TKPRGKGTGL GLSISHSIVK DHGGKLLIDS
     VEGEFTDITI VLPSV
//
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