ID A0A136NPE1_9BACT Unreviewed; 962 AA.
AC A0A136NPE1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=UZ10_BCD003000055 {ECO:0000313|EMBL:KXK47983.1};
OS Bacteroidetes bacterium OLB10.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1617421 {ECO:0000313|EMBL:KXK47983.1, ECO:0000313|Proteomes:UP000070480};
RN [1] {ECO:0000313|EMBL:KXK47983.1, ECO:0000313|Proteomes:UP000070480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB10 {ECO:0000313|EMBL:KXK47983.1};
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: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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:KXK47983.1}.
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DR EMBL; LNBX01000005; KXK47983.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136NPE1; -.
DR STRING; 1617421.UZ10_BCD003000055; -.
DR PATRIC; fig|1617421.3.peg.55; -.
DR Proteomes; UP000070480; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 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; 1.20.120.160; HPT domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat 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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF13424; TPR_12; 2.
DR Pfam; PF13181; TPR_8; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR PROSITE; PS50005; TPR; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:KXK47983.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Signal {ECO:0000256|SAM:SignalP};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000313|EMBL:KXK47983.1}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..962
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007477066"
FT REPEAT 123..156
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 203..236
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 460..684
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 708..833
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 866..960
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 764
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 905
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 962 AA; 108486 MW; DC1B7225270D1A95 CRC64;
MDKKYLLLLF IILHVWSASF AQDPSKLNEN FSELFDAKND SDKVDAYSHL GFNFSLLNPD
SGIYFSKKGL ELARKINYVK GIGDCYNSLG WCYSKKGMNN EAGKYLEQAK IYFEKTGNNC
YVSVAVGNIG NLYFNQNRYA EALENFLRSV ELSKNCPDKG FKSSKLYAIG AVYNSQKEYK
KAIAWFREAN VFNFANADTV KMAECINGIG NAWLGLQQYD SAMFYFHQSV KLFEDNNNLN
GIAYSNESIG GVYQEQKNYT KALEHYEIAL KNFRALNSRN DECYELITIG ETYEQKGDLK
AAILCQQRAL QIADSNSYLS LKQKALTSLS RLSAAKNDYK SAYEYFRQAS AVNDSLGLQQ
QQIKLNELKT KFETEQKDKE IALIKKDKEL QEAMALKQRQ LKNIFIAGAV VLLFIALGIY
NRYNIKRKAE IQLTQKNKLI QEEKERAKQS EEFKQQFLAN MSHEIRTPLN AICGMTELLS
EEELSEQQKK YIDVISASAA GLLSIINDVL DLSKVEAGKL ELEKIPVDIR KLTQEVYNAF
EYRAGQKNIS FATDVDAGVP QVIRSDAFRI RQILVNLLGN AFKFTEKGSV QLTVKSSPLQ
NHSDNRILIS FSVADTGIGI LPENQEKIFE SFIQSDTGTA RLYGGTGLGL NISKNLATLF
GGTITLDSTP GKGSVFTFSM PCEVFTASES EQPTNHAATV ADLKKEIHVL LIEDNVYNRM
LATDALEKKI ENIKINVFEN GRQALAFMQT QNREIAYDTV ILLDVQMPDM DGYEVARQIR
NNASNPFCAT PIIAVTANAF KEDIERCKAA GMNDVIAKPY KTNVLVQAVL KYAGQTATST
IEQTTAVDYK QEITNIDYLY EFTGGDMDEV KKYAEIFREA IPQRIEEAEK LLRNGESDAV
IRILHSIKPM IVSFGLTDCE TIITHLEQNR KNIKPNQLLP DFIKIRKQSL AAVDELSRNF
NI
//
