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Database: UniProt
Entry: A0A136MRR1_9BACT
LinkDB: A0A136MRR1_9BACT
Original site: A0A136MRR1_9BACT 
ID   A0A136MRR1_9BACT        Unreviewed;      1396 AA.
AC   A0A136MRR1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=UZ16_OP3001001500 {ECO:0000313|EMBL:KXK36527.1};
OS   Candidatus Hinthialibacteria bacterium OLB16.
OC   Bacteria; Candidatus Hinthialibacterota.
OX   NCBI_TaxID=1617433 {ECO:0000313|EMBL:KXK36527.1, ECO:0000313|Proteomes:UP000070296};
RN   [1] {ECO:0000313|EMBL:KXK36527.1, ECO:0000313|Proteomes:UP000070296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB16 {ECO:0000313|EMBL:KXK36527.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (NOV-2015) 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KXK36527.1}.
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DR   EMBL; LMZT01000071; KXK36527.1; -; Genomic_DNA.
DR   STRING; 1617433.UZ16_OP3001001500; -.
DR   PATRIC; fig|1617433.3.peg.1620; -.
DR   Proteomes; UP000070296; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00130; PAS; 2.
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; 4.
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; IPR007895; MASE1.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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; PF02518; HATPase_c; 1.
DR   Pfam; PF05231; MASE1; 1.
DR   Pfam; PF08447; PAS_3; 2.
DR   Pfam; PF13426; PAS_9; 2.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 4.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 4.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        42..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        88..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        123..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        156..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        196..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        227..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        251..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          395..447
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          529..581
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          663..715
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          718..785
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          788..840
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          1030..1255
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1277..1393
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         1328
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1396 AA;  155911 MW;  A7C078887E03FBDF CRC64;
     MRIHASTMNP FLRFILVVIS SFAGYLACSR ISLMLLTQPE NISAFWPPVG ILFGLLMVIP
     RLHWAGILTG SFCGNVVANM LIGKSFPISF IFSIGDLGFA YLFSELAVRY LGRPVTLNSL
     REIFHILGLG GFGISTGCAT WGALTLWLNQ PVESFWLLWA CWWSADIMGI LIFTPVCLAL
     IPGGYREIRS MNRARILEGC ALLAVFSLLV LGIFGNRYES TRILGPLPFT FVPVLLISAI
     RFGVRGAALT TSAFGISSVI FTVNGFGPFA SIFHSASEAI FRLQAFLAIS NVSTLVVAGS
     IAERKKSLDD LARTERLYRK AIEIAGAVPY FGLYGKKDFE FVGEGIDKLT GIPASRFDHQ
     KLADITLEIH PLGELNGKNA DDAIETVREH HEIPWHADYR IQLPDGDIRW LANSAVQVLD
     GKGNAIGSLG ILQDITERKK SEQAIARSEE LYRSAIDGAG AVPYYRDYKT DARGEILSSR
     YSFMGKGIER ITGYTPEEFT LELFEEILTD EIRYNPASAP GQSEIQPQFR AEYALRHKNG
     SICWVSDAAV DIHNEQGHFI ASLGILQDIT LRRQAEEEIR KTDLLYRSAI EGADAVPYYL
     NHRTVAYDFL GDGILNLTGF SSKEFTPEVF QTLILDRVFH AEMRGLTREQ AMHRMRTEIG
     SCWRADYRIK TRHGEERWIS DSAVQVLDDK KNVIGSLGIL MDITDRRKSE DSIRIRDRAL
     SFALNGIMIT DASVPENPIM FVNPAFTKIT GYQLEDMAGK TPYFLYEHGD HQEGLDIIRR
     AFTEGTAAEA VSPINRKDGQ TIWGDIFIAP VRNDMDQVTH FICIQNDITD RMRIEKDQKV
     LIDGLRSIVG IADELLDCPD EDTITRMAVE LGRERLGMER LAFHRMENET LFGTYGTDAQ
     GNTIDEKSYK KQFDRKWFEA LKIETGSNYQ WYYIDGGHYS WNNGEMDQIG SGWVVMTPVA
     SSQKWQGVFF NDTALSGKPY DPTRQELLAV YASLFSNIIE RRRSEEARSK LEAQVHHTQK
     LESLGVLAGG IAHDFNNLLM GVLGNASLAL MELPPESPAR ESVNHIEKAA MRAAELARQM
     LAYSGKGRFV IQKINLSKLV EEMTHLLQVS ISKKVFLRYN FADNLPAIEG DATQIRQVIM
     NLITNASDAI GDKSGVITIT TGLIETDSTY LESTYLKDDL PGGYYVFLEV SDTGCGMDEE
     TRARIFDPFF TTKFTGRGLG LAAVLGIVRG HKGTVKVYSE AGRGTTFKIL LPCCDSQEDT
     QENHVESTRK DWVGTGTILI VDDEESVRYI SKRILESHGF KVLTANDGRE GVKAYEAQKE
     AIDLVLLDMT MPHMDGEEAF RELRLINPDV HVILTSGYTE QEATARFTGK GLAGFIQKPF
     LPSSLLEIVR NKLSTS
//
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