ID A0A0K9FGL6_9BACI Unreviewed; 914 AA.
AC A0A0K9FGL6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ACZ11_00565 {ECO:0000313|EMBL:KMY33615.1};
OS Lysinibacillus xylanilyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=582475 {ECO:0000313|EMBL:KMY33615.1, ECO:0000313|Proteomes:UP000037326};
RN [1] {ECO:0000313|Proteomes:UP000037326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23493 {ECO:0000313|Proteomes:UP000037326};
RG Consortium for Microbial Forensics and Genomics (microFORGE);
RA Knight B.M., Roberts D.P., Lin D., Hari K., Fletcher J., Melcher U.,
RA Blagden T., Winegar R.A.;
RL Submitted (JUL-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:KMY33615.1}.
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DR EMBL; LFXJ01000002; KMY33615.1; -; Genomic_DNA.
DR RefSeq; WP_049662704.1; NZ_LFXJ01000002.1.
DR AlphaFoldDB; A0A0K9FGL6; -.
DR PATRIC; fig|582475.4.peg.3663; -.
DR OrthoDB; 9790669at2; -.
DR Proteomes; UP000037326; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd19410; HK9-like_sensor; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR007891; CHASE3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KMY33615.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 13..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 212..266
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 511..743
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 792..909
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 428..501
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 842
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 914 AA; 103267 MW; 68359C97EDC944BB CRC64;
MFNKLKVGIR RKITLGYIVI ILCLLASVLI LNNQIISLQK ERNYIIKNNS HIHAVTNCIE
KYILDMESSQ RGFVITGEPS YLETYYEAGE KWRSDFNELY QLFENKPTQQ QKLNEIKATI
EHWITTSGEP SIEFKKENKA EAIWELYKVD VGRKDMETVR AQFESLRSEV NASMQAKVND
LDKRNSIVTH TLLGILVFIS VVAIIIANGI SRSIVKTLTQ VTQTIQEIAA SKSSQKGRIH
VRTNDEINDL AVATNELLDI LERREWLQLN IAEIVTKYQG ICAITKLAET FLSEIAQKTQ
SSLGAFYVRE TTDNNIQFVK KAAFADARDD VGIESFKLGQ GLIGQCALEK KILIYNDIPE
DFRLIGTSLG EVPPKSIFIV PIIFENDVIA VVELATMTGF NEQQQRLVKQ VIETFGLTIN
SVLGRMEIVR LLNESRAMTE ELQMQSEELQ AQSEELQMQT EELTVINEQL EERTNEAELK
TRELEQAKRE LEESAEQLLL NSNYKSEFLA NMSHELRTPL NSILILSEML AENSQSNLSD
EEAEFAKVIH SSGEDLLALI NDILDLSKVE AGKLDISFDE MNMSEVPVQI EQTFAPVATK
KNLQFHISKE KNVTDIFFTD EKRFKQILKN LLSNAFKFTE QGSVNLEIKQ LGQEQLTNNM
QDLSADWLEI TVTDTGIGIP KDKHQLIFES FQQADGAIVR KYGGTGLGLS ICKELARLLG
GWISLQSEEG QGSTFTLTIP SLPNGIEEQK YLELAIHEVG ATNEVHELEE EEQLSEVQEF
SQHEVEVFQG KNILIVDDDY RNIYALKNAL EKRGMDILVA KDGIECLDIM QSNGGIDLIL
MDIMMPNLDG YETMSIIRKQ LNITDLPIIA LTAKAMKNDR DKSLEAGASD YISKPLNLDQ
LISVLRVWLV SKGS
//
