ID A0A1Z5SHI0_9BACT Unreviewed; 878 AA.
AC A0A1Z5SHI0;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CAP35_00625 {ECO:0000313|EMBL:OSZ81806.1};
OS Chitinophagaceae bacterium IBVUCB1.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae.
OX NCBI_TaxID=1985173 {ECO:0000313|EMBL:OSZ81806.1, ECO:0000313|Proteomes:UP000194327};
RN [1] {ECO:0000313|EMBL:OSZ81806.1, ECO:0000313|Proteomes:UP000194327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBVUCB1 {ECO:0000313|EMBL:OSZ81806.1,
RC ECO:0000313|Proteomes:UP000194327};
RA Orr R.J.;
RT "Draft genome sequences of novel bacteria, isolated from environmental
RT samples.";
RL Submitted (MAY-2017) 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 -!- 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:OSZ81806.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NFUW01000001; OSZ81806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5SHI0; -.
DR STRING; 1985173.CAP35_00625; -.
DR OrthoDB; 9811889at2; -.
DR Proteomes; UP000194327; 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; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF17874; TPR_MalT; 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; 6.
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.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000194327};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT REPEAT 102..135
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 182..215
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 374..595
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 620..740
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 783..878
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 671
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 822
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 878 AA; 99132 MW; 5356D1718BE0811B CRC64;
MDTQRYKELQ KEYEIVKDER ARIDIYIQMV VEVRSSDVEQ ALDMANEIID RSEAIGYRLG
KGRGMNLKGW CYWQQGEYDN GVDILQDALK ISHDINNKPL QARVLNNLGY IYRDRGDLAD
ALNHFEAALK INEKLGDEVA QSVNLSSIAY LLYDLNDYDN ALEFALRCMP IFEKANDLHR
LNALYHILGN IYFKQEELQQ ALHYFEENLR LSEPDSSMHA LAISGLGKVC YAMNDFENAR
INLVNALKQS EELGNVEVQI ICHFYIGRMM MDEGNYRQSQ QHMNAAFELA DEYSRRHDVM
SVHEALSMLY DKMGDIPKAF HHLKAYEQLK EDIFKQTTFN KIRNLQTRQQ VELAQKEKEV
AERTAQLKQQ FMANMSHEIR TPMNAIVGMT SLLQSKNPLP EQVKYLKAIQ QSADNLLVII
NDILDLSKIE AGKIVIEQTD FSLREVIHSV RDMLMLKAEE KKLNFKVSVE EGIPARVTGD
PTRINQILIN LAGNALKFTE NGFVAINVTI QKKQDKKYWL KFDVADTGIG ISPDYVGKIF
ESFTQAGTDV ARKFGGTGLG LTISKQLTEL MGGEISVTSE LGKGTTFTVV LPITESDVQV
VEQKSSVLDA QSMQRLNKVK LLLVEDNEFN RMVAEDTLKE LLPNIKIDIA INGQEAVNRV
QQQQYDIVLM DIQMPVMDGV TATRNIRTTL PAPAKDVKII AMTANVLQED VNQYFNTGMN
AYVSKPFQAD ELLLKMAAVL DGQAPANANN GTVKNTIVAE PAMPSLPDVI TDMQFLKQFT
GGNDEKMAKY VGMFLENGPK LLTTIQQSLQ TKDYGAVKIA AHSMKPQLSY MGVKEDVSHI
FLIEQTAGES AHYDRLPTLV ANLARVCEKA FAELKKQQ
//