ID A0A3N4M647_9BACT Unreviewed; 987 AA.
AC A0A3N4M647;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EG028_25145 {ECO:0000313|EMBL:RPD38555.1};
OS Chitinophaga barathri.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1647451 {ECO:0000313|EMBL:RPD38555.1, ECO:0000313|Proteomes:UP000279089};
RN [1] {ECO:0000313|Proteomes:UP000279089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLT18 {ECO:0000313|Proteomes:UP000279089};
RA Zong Y.;
RT "Chitinophaga lutea sp.nov., isolate from arsenic contaminated soil.";
RL Submitted (NOV-2018) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00110}.
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:RPD38555.1}.
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DR EMBL; RMBX01000015; RPD38555.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4M647; -.
DR OrthoDB; 9811889at2; -.
DR Proteomes; UP000279089; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
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; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR007891; CHASE3.
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; 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 InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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; 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); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
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}; Reference proteome {ECO:0000313|Proteomes:UP000279089};
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 177..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 217..288
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 350..407
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 421..474
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 492..713
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 738..852
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 888..987
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 787
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 987 AA; 112052 MW; 92ED2AD7204856DF CRC64;
MKKISSPVII VFVAAIVSVA WFAWSAWFSD ADAIKRNERI QLTNDKIRLL ERVAYTVKSL
ESSVRAYVIT GDSGFLTRED FTETQLRTPV ENLQFLASDS REAHAMDSLR AMVYQRIVYF
NYLISSTRES PVIAGAMIRP VQTPAPPDPL TSLIDRLLED QYSHMEARLS SSLPNRLPFL
VTLTASALAL GVIFWGLYKL VKDMRKTKAS ESALRTSEAK YRRLIEDAGA TMFTTNRGGF
FKYVNSKALD LTGYTPQELI DKQYTMLIDP PEQQRLREHY EKQAFEGTTE SSLRFPIRCK
NGDQKWVEQH VVLLRQHGIF SGYQCIVKDI HAKKMADEEV VKTKNEMNTL HSRLQSILLN
SPSMIFIKDI NSKYVLINRR FEEVFGIKSE NILGRADKDF PSKLKPEKSI ESDRAVLLHE
KPVESEDSIE INGKTHYFFI TKFPLRDHTH RVYGLCGIAT DITERIQHEH ALIDERKRAI
DARRAQEFFM ANMSHELRTP LNGILGFTYL LEQTATNPQQ SEYVREILDS ANNLLALVND
LLDFSRIKTG RMVLEHAAFD LRELIAQKAD KYRPLAEKKG LQLLCDMQEN MEGLVLGDPL
RLKQILNNLI DNAIKFTENG SISLSVSIEE ENEKQLKYAF ELKDTGIGIP GHLHHEMGET
FIQVHAGNDR KHGGTGLGLA LVRQLVGLHQ GTIHICNNPE GGTIIRFIIP YNRQVQEPVF
VPEASKETLL LPPLQGKNIL LAEDNLVNQK LAIRTLANAG AAVELAENGL EALEKLRHHK
YDCILMDIQM PEMDGLEATR KIRDSGSAIP IIAMTASALK GDRERCLLAG MNDYISKPFI
PNDLFQKILE ALGERDPVFA KFTGPDYEEQ RVPSLVDLRY LRDVVDDNPE YMLDILNTFL
ERTDSMLTNM ENSAQLEAWD ETSQHAGLLR SSLMVVRIQP LSAIVHEIEQ QARNRESLHT
VLPNIHLAIK LYKDAHSVLL KEVNKLS
//
