ID A0A1H4D376_9BACT Unreviewed; 1292 AA.
AC A0A1H4D376;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05660909_02936 {ECO:0000313|EMBL:SEA67205.1};
OS Chitinophaga terrae (ex Kim and Jung 2007).
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=408074 {ECO:0000313|EMBL:SEA67205.1, ECO:0000313|Proteomes:UP000199656};
RN [1] {ECO:0000313|Proteomes:UP000199656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23920 {ECO:0000313|Proteomes:UP000199656};
RA Varghese N., Submissions S.;
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};
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}.
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DR EMBL; FNRL01000012; SEA67205.1; -; Genomic_DNA.
DR STRING; 408074.SAMN05660909_02936; -.
DR OrthoDB; 9809670at2; -.
DR Proteomes; UP000199656; 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; cd00130; PAS; 4.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; 3.30.450.20; PAS domain; 5.
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; 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; IPR013655; PAS_fold_3.
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 NCBIfam; TIGR00229; sensory_box; 4.
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; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 3.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 4.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 4.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}.
FT DOMAIN 33..82
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 134..185
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 332..383
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 384..430
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 468..520
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 521..590
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 664..887
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 903..1023
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1048..1166
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1200..1292
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 504..531
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 953
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1099
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1239
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1292 AA; 146327 MW; A1F68467673B2770 CRC64;
MVNQSVPRDG DNLDYFHKFF LLANDLLCLV GGDGSLKAVN PAFSKLLGWK QDELIGRSVF
EILHPQDVES SAQQLQGLNE GRDTVNFINR MRSSSGNYIY LQWMASPDAA SGDIFAIGRD
ISQVMEKERQ LQENEHQFRI FFNNSRGMMC MHDLNGKLLA VNLASAESLG YKPEELIGST
LWDIVPEKFG AGVFEYLAAI ERDKEVSGLM HTRHRDGSVR IWLYNNVLEY SIEGNPYVIA
NALDITERHA LEKDLKWTTQ MLEQTNSVAR IGFWQYDIVK QKIYWSDVTC SIHDVPDGFV
PELDKAMGFY KPASRRILEA AVERAINQHI PYDLELEIVT ARGIETWIRV IGSPVVKDGK
CVRLFGTFQD IDRQKRLEEE IQRSRKLLED LLQSAIHVSI IATGLDGTIT LFNKGAELML
GYNSREVVGK HTPVTIHDPF ELEERAMAYG VSIPEVFALE AAQEMDASQQ EWTYIRKDGS
SVNVSVAISA IRNVDNELTG YLHIATDISK RKRAEQQLQE EKSKLSAFVQ QTPAAVVMLD
RELRIIAFSD AWKEQTGLDS DQLYGKNVQE FLPEVPSEFK QVYRNTLAGR IEKNEEFIWR
PPGWTRDQHL RWEIRPWYLA GGRIGGITIL LEDITENALR QEELRQAKLL AEQASIAKSE
FLANMSHEIR TPLNGIIGFT DLVLKTRLSE IQHQYLSIVN QSAGTLLNII NDILDFSKIE
AGKLELDIQK TDIYEMSSQV SDMVKFQAQS KGLEMIYDIS PELPRFICAD QLRLKQILVN
LLSNAVKFTE KGEVGLKIYP VSAATADNFR TIRFEVRDTG IGIRPERQGK IFEAFSQEDL
SITKRYGGTG LGLTISNKLL ALMNSRLQLD SELGAGSTFF FEINLETADG PPLNWDNIEA
VKRVLITDDN EHNRIIIRQM LMLKNIEVDM ARNGFEALQM LMEGRVFDAI LMDYHMPVMD
GLETLRKMRQ MTSQTGISIP VIFLYSSSDD ETVIRACEEL QVEQRLVKPV KMQELYHALA
RLCTTGAKND REESADQQAW GPEQRLLKVL LAEDNSVNML LIKTIIARSL PQSAILEAKT
GVEAVSLFTK EQPDLVFMDI QMPDMNGYDA TRRIRELYPD RATPIIALTA GNTKGERERC
LEAGMDDFLT KPFLEEDILK MVNKWVNKNH EKTPGEPETP SPQPLDITVL MGYLGSKDDS
DPVLRETLEL LLEDCKAARQ ELQDSDMTGN EKRIAQICHS MKSVTTYAGL KDLEKVILET
ESQGATKEQL QQLDIELEKA VASIEQTLAK LP
//
