ID A0A1L3ZT90_9SPHN Unreviewed; 795 AA.
AC A0A1L3ZT90;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BSL82_05555 {ECO:0000313|EMBL:API58838.1};
OS Tardibacter chloracetimidivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Tardibacter.
OX NCBI_TaxID=1921510 {ECO:0000313|EMBL:API58838.1, ECO:0000313|Proteomes:UP000182063};
RN [1] {ECO:0000313|Proteomes:UP000182063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JJ-A5 {ECO:0000313|Proteomes:UP000182063};
RA Lee H., Ka J.-O.;
RT "Complete Genome Sequence of alachlor-degrading Sphingomonas sp. strain JJ-
RT A5.";
RL Submitted (NOV-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};
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DR EMBL; CP018221; API58838.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L3ZT90; -.
DR STRING; 1921510.BSL82_05555; -.
DR KEGG; sphj:BSL82_05555; -.
DR OrthoDB; 9796100at2; -.
DR Proteomes; UP000182063; Chromosome.
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 CDD; cd00130; PAS; 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; 3.30.450.20; PAS domain; 1.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 3.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000182063};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 286..355
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 420..643
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 669..783
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 719
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 795 AA; 84492 MW; 1DEC2D81B9AF2604 CRC64;
MLTMAAAAST VAALASAVLI SWALQDVASG AIFGAVILGA SALTFAVTRG RTAARVAATA
TDWTATRLTL DAMGGAAAIC DVNGRLVCAN QAWAEKAGGY RAPAELAGTD AEAVDAVARA
QQQAWQQGSA TVVFAPAEGS GRRVLSIKRM EGKDECCLWL LEERIGSAVR DTARALISGD
VGEWFSRAGV SAVITDSEGR IIAANATFRT TIGRDDLVEQ EATLTSLLDL DQSGVVRVLD
GEGRRDPVRV VELALGGEPH EPRTYLFLLL DETGGDYGRA AGAAESSASI PALLGTLPLG
LALTDRDGRF RFMNQAFCRA AGIGEGEEVL YPSDLVMEDE KAMVADAIRK MATGQPTLRD
LRIRLKAAPE EPIVLTLARV TGFGLPAVIL YLADNSEQEK LERQVAQATK MQAVGQLAGG
VAHDFNNILT AIIGYCDLML LRHGPGDSDF DDITQIKQNA NRAANLVRQL LAFSRQQTLR
PQVLQISDVV GELSHLLKRL LGERITLTVK HGRSLGAVRA DPGQLEQVIV NLAVNARDAM
PEGGELSIST FAVSAADARR LGADILPPAD YTALKVSDTG AGIPADILAN IFEPFFTTKE
VGKGTGLGLS TVYGIVKQTG GYIFAESEPG HGASFTIYLP VHAAREGTER PAVPTGSKAQ
GNELWGVGTI LLVEDEATVR AVAERALVRK GYRVVTAANG VEALERLAEE DHIDLLISDV
VMPEMDGPTL VAKTREERPD LPIVFMSGYA EEQLRRSISV PGFAFLPKPF SVQQLGEAVR
DALARAQEKR EREGA
//