ID A0A166XR60_9GAMM Unreviewed; 511 AA.
AC A0A166XR60;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=N475_11290 {ECO:0000313|EMBL:KZN40705.1};
OS Pseudoalteromonas luteoviolacea DSM 6061.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1365250 {ECO:0000313|EMBL:KZN40705.1, ECO:0000313|Proteomes:UP000076643};
RN [1] {ECO:0000313|EMBL:KZN40705.1, ECO:0000313|Proteomes:UP000076643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6061 {ECO:0000313|EMBL:KZN40705.1,
RC ECO:0000313|Proteomes:UP000076643};
RA Vynne N.G., Mansson M., Gram L.;
RT "Comparative Genomic and Metabolomic Analysis of Twelve Strains of
RT Pseudoalteromonas luteoviolacea.";
RL Submitted (JUL-2013) 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:KZN40705.1}.
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DR EMBL; AUYB01000093; KZN40705.1; -; Genomic_DNA.
DR RefSeq; WP_063357308.1; NZ_AUYB01000093.1.
DR AlphaFoldDB; A0A166XR60; -.
DR STRING; 43657.S4054249_00265; -.
DR PATRIC; fig|1365250.3.peg.1483; -.
DR Proteomes; UP000076643; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
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; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000076643}.
FT DOMAIN 92..144
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 155..369
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 391..508
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 441
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 511 AA; 57190 MW; 67D1A2AB37B55E09 CRC64;
MHRLEKELYA HIQKSPEIFN FLVECSLDGF WYWDLENPAQ EWMSPKLWQT LGYDPNTKQH
LVSEWQDIIN QDDLKLAMEN FEKHKADPTY PYDQIVRYTH ATGKTIWIRC RGLIIRDEND
KPVRMVGSHT DITEIKESER RAIEALEARE QFFARMSHEI RTPLFGILGI AGTLKSAVVN
DKIAQDISTI LSCGEQLQSL LNDILTLAKL DAEKLSTSIE VVDLASVFSH IHELYSAAAD
DKQLALEVET DNVTGMFVKT DKVRLTQVLS NLVSNAIKYT KTGSVKVQAK FEREECTISV
IDTGVGIKDV DAIFNAYTQE DTSYESMVSG SGLGLEVVSQ LCELLNYDLS FNSEVDVGTQ
VTISMAAVQA QTPSAEQEKV SEPLPELSIS RTLIVDDNAL NQVITTKMLS SICPDIEKAS
DGYEALQVIS KSPPFDLILL DINMPKMNGY EVLALINTMS LDTQPYIIML SADAFEATQQ
KCLELGADGY LTKPFTQQEL TEALSTMPVS K
//