ID A0A0U2PDF1_9ALTE Unreviewed; 947 AA.
AC A0A0U2PDF1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AT746_01420 {ECO:0000313|EMBL:ALS97069.1};
OS Lacimicrobium alkaliphilum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Lacimicrobium.
OX NCBI_TaxID=1526571 {ECO:0000313|EMBL:ALS97069.1, ECO:0000313|Proteomes:UP000068447};
RN [1] {ECO:0000313|EMBL:ALS97069.1, ECO:0000313|Proteomes:UP000068447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YelD216 {ECO:0000313|EMBL:ALS97069.1,
RC ECO:0000313|Proteomes:UP000068447};
RA Kim S.-G., Lee Y.-J.;
RT "Complete genome of Lacimicrobium alkaliphilum KCTC 32984.";
RL Submitted (DEC-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};
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DR EMBL; CP013650; ALS97069.1; -; Genomic_DNA.
DR RefSeq; WP_062475429.1; NZ_CP013650.1.
DR AlphaFoldDB; A0A0U2PDF1; -.
DR STRING; 1526571.AT746_01420; -.
DR KEGG; lal:AT746_01420; -.
DR OrthoDB; 9804645at2; -.
DR Proteomes; UP000068447; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000068447}.
FT DOMAIN 251..303
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 463..539
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 594..665
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 723..942
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 153..183
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 947 AA; 107786 MW; 143AA7B7C3D2D8A7 CRC64;
MQPPAIPENE QLRLRALVES GLLDSAPEER FDRLTAMAKA LFSVPIVLVS LVDRDRQWFK
SRQGLDATET PRDISFCGHA ILQHQLFVVE NALEDPRFSD NPLVVGAPHI RFYAGAPIRD
EGGYNLGTLC LIGTEPQQLS KKQQSMLRDL AVLVEKEIQY QDVRRLNRQL RESRDQYASL
VENIPGITYR CLHDKSWTML FMSREIDPLT GYPVSDFIQN AKRSYASLIP EEYHQYLSDM
VDKAIAQKDA WHIEYPIRHA DGKLRWIEER GNAIYDEDDN VSCLQGFLLD ISREKAARDK
LQRQNQALNL LNKISFELSG ELQQVIERAL KLGCEFLNMD MAIVSEVLAQ TYVVRWFHSH
EPGQLHHEQR FALAETYCDI TLSQGKQVAI AHMRESAFSS HRCYQTFGME SYIAQPLKVD
GKLFGTLNFT SASPRLGGFD EIDRLFVSLL ERWLGAKLDW HQQRRKLKNL VEQVPGMIYQ
YRQWPDGRIS LPYASPGIEE IYGLTAQELE HDASALYSRI HNEDVERVSQ GIAQSQQQLS
LWHQQYRITN AAGEVEWIEG RAVPVRLEDG STDWYGYIAS IQAAKQIELT LESSEQRLRA
LFELSPIGIA LIDFSTARLL DCNAALLHPS GYRRGELLEL HMMDLVPPDY QYLRHQILEQ
LQSQGRFDPV EAELQCKGGR TYPIRLQGVK ITDQEQNPLL WCLVEDISEH KRIERMQKEF
IATVSHELRT PLTSIKGALS LLGGGMVENL PEKAKSLLSA AYRNSNHLGE LIDDILDLEK
LTAGAMIFDT QTLQVSEVMR EAKELYQHYG QKRGIRVRLL QPEGGHHVRA DKKRLLQALG
NLLSNAIKFS PEQDEVTVSV INEQQQVRIL VQDQGPGIAE AFKDRIFSRF AQADSSDTRK
KGGTGLGLAI TRELMEQMGG SVDFVSVPGQ GTTFWLQLPQ AEQQLES
//
