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Database: UniProt
Entry: A0A2X3Y2L3_9STRE
LinkDB: A0A2X3Y2L3_9STRE
Original site: A0A2X3Y2L3_9STRE 
ID   A0A2X3Y2L3_9STRE        Unreviewed;       456 AA.
AC   A0A2X3Y2L3;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=arlS_2 {ECO:0000313|EMBL:SQF41062.1};
GN   ORFNames=NCTC12278_01658 {ECO:0000313|EMBL:SQF41062.1};
OS   Streptococcus ferus.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1345 {ECO:0000313|EMBL:SQF41062.1, ECO:0000313|Proteomes:UP000249495};
RN   [1] {ECO:0000313|EMBL:SQF41062.1, ECO:0000313|Proteomes:UP000249495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC12278 {ECO:0000313|EMBL:SQF41062.1,
RC   ECO:0000313|Proteomes:UP000249495};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-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};
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DR   EMBL; LS483343; SQF41062.1; -; Genomic_DNA.
DR   RefSeq; WP_018030667.1; NZ_LS483343.1.
DR   AlphaFoldDB; A0A2X3Y2L3; -.
DR   STRING; 1123303.GCA_000372425_01345; -.
DR   KEGG; sfer:NCTC12278_01658; -.
DR   OrthoDB; 9762826at2; -.
DR   Proteomes; UP000249495; Chromosome 1.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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   PANTHER; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1.
DR   PANTHER; PTHR45528:SF9; SENSOR HISTIDINE KINASE YRKQ; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249495};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SQF41062.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        7..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        148..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          169..221
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          243..453
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          206..233
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   456 AA;  52007 MW;  F70EA0510A492ED4 CRC64;
     MGIVRKNFLI VTSMIIATVL VLLAVIYYAM PIYYNQAKQV EIKNDYQAIV KQLDGKSTEK
     LLSQIATYDK TNPNLLLTLM DDSGKILYPD ASDKEAADRR KTYLEKGQFD QIGSWSELIA
     SSEGDAYIVQ AEYGFQSLSG ISQILLTFYP FILVFIVLLA SLVAYVYSRL SNKRIQTISE
     TTRQMRALEE GLACQISGQD EIANLAQNIN QLYNHLLQSI AELKQENQRT VERERQQADF
     LRITSHELKT PIASSLALVE GMLYNVGDFK DHDTYLRKCR DILQEQSVLV QSVLDATNLD
     IGVKSHQETI DVKSLIEQNL DSYYILAETH SYQFSSTLTS YRVTANPAYL LKAIKNLLDN
     AFRYTRAGGV IHLSLSEGRL ILENQAEQLL TDEELKHIFQ PFYRPDFSRD RKDGGTGMGL
     YMVQQILDQH GFSYHFKRSG DKMRFILFLD RASIQD
//
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