ID A0A075NTL1_9ALTE Unreviewed; 954 AA.
AC A0A075NTL1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EP13_04015 {ECO:0000313|EMBL:AIF97929.1};
OS Alteromonas australica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=589873 {ECO:0000313|EMBL:AIF97929.1, ECO:0000313|Proteomes:UP000056090};
RN [1] {ECO:0000313|EMBL:AIF97929.1, ECO:0000313|Proteomes:UP000056090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H 17 {ECO:0000313|EMBL:AIF97929.1,
RC ECO:0000313|Proteomes:UP000056090};
RA Gonzaga A., Lopez-Perez M., Rodriguez-Valera F.;
RT "Genomes of Alteromonas australica, a world apart.";
RL Submitted (JUN-2014) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP008849; AIF97929.1; -; Genomic_DNA.
DR RefSeq; WP_044056121.1; NZ_CP008849.1.
DR AlphaFoldDB; A0A075NTL1; -.
DR GeneID; 78254099; -.
DR KEGG; aal:EP13_04015; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR Proteomes; UP000056090; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
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; 2.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 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; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
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; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AIF97929.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000056090};
KW Transferase {ECO:0000313|EMBL:AIF97929.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 18..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 435..508
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 509..562
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 580..801
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 825..944
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 874
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 954 AA; 106274 MW; AC323FC8555D668B CRC64;
MRAPPLRKLL LKSMLPRLAS VILIISILLL GITLYFVRLQ VSDVQKQSLE GLQQDLSFIV
SDTTRQLSDL AANDILINSL VDIEQRDSYL PMFFRSLNLT QANNVSFALY DFSGKKLIDK
NFDGTLPNNL QNAWQQETLG ASQAYSSISR YGVLISVPVL LGGVAEGALV MYVDSLQALL
APYPRLTNQI VTDNTGTILF SSDTEKFVPS SLFTDVDVEN FVVEMVPWEN LSLYSIKPSS
EAYRSLYSLA IVLCVMIIGI LLVGLHIVRT TGLLAENTLS NLYTDIENRI NTKQGQPRTS
STLEARELVN IREAFDKLLW DLTEVSVSNE QFSNVIDSMG DMLVVVDTAN AVILSNRRFE
AFCADQYGEV EGTVKFVVNK LNNKSSDELK HFSIQDGHEK QIRWGKTALK DANENVRGSI
FVGLDITTQR SLESHVQILN HAMDEATVSI VISDVRRTGQ PIIYTNHAFS ELTGYSREEI
IGKNCRLMQG EETEQKNIAA LRQAIIDNRP IETTILNYRK DGSTFFNRLI LTPVKIDGVV
THYIGFQQDV TQQRQAELYL QEAKQKAEES ARLKSGFLAS MSHEIRTPIH GISGVLQLMS
DSPLSDEQKH YLSLAKFSIQ GLLHIVNDIL DFSKIEAGQL QIEAQPFDIL EELESIQSQF
AILCQEKGLA LHFHFNLQGY HVVIGDAVRF RQILSNLIGN AVKFTQNGAI DVTTSIESVP
DGNLRLVCNV QDTGIGIADE KQSGIFNVFT QEDISTTRQF GGTGLGLSIS KQLCELMQGS
INVESTKGEG STFTFNILLQ EGDDSLLLPA HDTRAFKPTK GSKRKILIVE DNDINQIIVK
QHLSHHTTLS AKSGIEALQA LVKMKVTFDV ILMDCQMPDM DGFEATRRIR AGDAGERYVD
IPIIALTANA MKGDREVCEE AGMNDYLSKP FDAKDLLDKV QYWAERSKEA LDSQ
//