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Database: UniProt
Entry: A0A1X1ZNE2_9MYCO
LinkDB: A0A1X1ZNE2_9MYCO
Original site: A0A1X1ZNE2_9MYCO 
ID   A0A1X1ZNE2_9MYCO        Unreviewed;       553 AA.
AC   A0A1X1ZNE2;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AWC19_08475 {ECO:0000313|EMBL:ORW24867.1};
OS   Mycobacterium palustre.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium simiae complex.
OX   NCBI_TaxID=153971 {ECO:0000313|EMBL:ORW24867.1, ECO:0000313|Proteomes:UP000193529};
RN   [1] {ECO:0000313|EMBL:ORW24867.1, ECO:0000313|Proteomes:UP000193529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44572 {ECO:0000313|EMBL:ORW24867.1,
RC   ECO:0000313|Proteomes:UP000193529};
RA   Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA   Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA   Olivier J., Enrico T., Nicola S.;
RT   "The new phylogeny of the genus Mycobacterium.";
RL   Submitted (JAN-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:ORW24867.1}.
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DR   EMBL; LQPJ01000100; ORW24867.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X1ZNE2; -.
DR   STRING; 153971.AWC19_08475; -.
DR   Proteomes; UP000193529; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR033463; sCache_3.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR016120; Sig_transdc_His_kin_SpoOB.
DR   InterPro; IPR039506; SPOB_a.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF17203; sCache_3_2; 1.
DR   Pfam; PF14689; SPOB_a; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   SUPFAM; SSF103190; Sensory domain-like; 1.
DR   SUPFAM; SSF55890; Sporulation response regulatory protein Spo0B; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ORW24867.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          431..543
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   553 AA;  58683 MW;  E93BB13EF12A15E3 CRC64;
     MRLATQVMLL QLVIVTLTLL VALVLFAWFN RHRLDLQYNR HALDIARVVS SSPTVINNIG
     RYDTEKLSPG PALIGELTTG PIQGIASRVE DRTHASFVVV ANMRGIKLAA PDRDTLGLSV
     RADITRALTG HEGTFHEATP LGRAIVAQVP VLEPGSGRVL GAVLVGISTK EFDDQFSRNL
     RVMAGIAGVL LLLGGAGSVV LARRWRGLTL GLRPDEITEL VRTQAAVLQG IGEGVLATDT
     AGRTTFVNDE ACRLLEIGTD TGRPVDEIGL TPRVLDVFKA ADSKPSLATV GERIVVVSAR
     PVSREGRELG TVLVVRDRTD VESLTRQLDA VQVMSTVLRA QRHEFANRLH LLTGLLHGGH
     VEEGLQYLEE LLGAGPLGSA LPGIDAIRDT YLQAFLAAKG AAAREAGVTL TIGENTWVPG
     RLVLPVDVTT VLGNLLDNAI DAVRMSGNAV KEVEVELLQE GTTLHITVAD SGDGVAPGFV
     DQLFTEGTTT KPDSGIPGGR GIGLALSRQI TRALGGDLLL ASAGNAELRL CGAEFIARLP
     GVMVEEAQWA TQT
//
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