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Database: UniProt
Entry: A0A1S2H7F6_9MICO
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Original site: A0A1S2H7F6_9MICO 
ID   A0A1S2H7F6_9MICO        Unreviewed;       486 AA.
AC   A0A1S2H7F6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BIU96_06820 {ECO:0000313|EMBL:OII05484.1};
OS   Curtobacterium sp. MCBA15_008.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Curtobacterium.
OX   NCBI_TaxID=1898736 {ECO:0000313|EMBL:OII05484.1, ECO:0000313|Proteomes:UP000180168};
RN   [1] {ECO:0000313|EMBL:OII05484.1, ECO:0000313|Proteomes:UP000180168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCBA15_008 {ECO:0000313|EMBL:OII05484.1,
RC   ECO:0000313|Proteomes:UP000180168};
RA   Chase A.B., Arevalo P., Polz M.F., Berlemont R., Martiny J.B.;
RT   "Evidence for ecological flexibility in the cosmopolitan genus
RT   Curtobacterium.";
RL   Submitted (SEP-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   -!- 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:OII05484.1}.
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DR   EMBL; MJGN01000056; OII05484.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S2H7F6; -.
DR   STRING; 1898736.BIU96_06820; -.
DR   Proteomes; UP000180168; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR   PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 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   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   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        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        156..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          174..227
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          235..486
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          423..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   486 AA;  50901 MW;  C9CFDF59F6193899 CRC64;
     MRPLRVLSLR SRITIGSTAI AAVVIVLLVL VMRFQVVSVV ASATRTLLDA DADPYVATLE
     VDSDPKLSAP GNAQLVAVVS PTGDIALSTM PPKVERALGS LTATEAGTSL IRVSGSEYRV
     VVEHPVNQAG RWTVVAARNS QAEAIVVDDL TSTLSLTGLA ILVAFGIASW ALATAALRPV
     NRMRREAERL SVAPERAELP VGPAQDELAS LATTLNAFLA RTRQATERER QMVSDASHEL
     RTPLAILTTQ LDLASLDGDD AAALAAHIER AKLSVARLSR LANDLLALSR IEESERRDQD
     GQEQPLTAWS DLGDEVMSAV DRVRLIASAK DITVDFDLEP PVTVGGSGPG IGGGSTEPRY
     RLDTGGMAQL VTNIAGNAVA ALPRGGGVFV SWRSAAGEGV LQITDDGPGV PESFIPVAFD
     RFTRPDEARK SRPNPDPATG GIPLPGGSGL GLAIVRAVAE RSGGTASLRN VRSGGLEVTV
     RIPEAS
//
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