ID A0A075P2V3_9ALTE Unreviewed; 713 AA.
AC A0A075P2V3;
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_11680 {ECO:0000313|EMBL:AIF99290.1};
OS Alteromonas australica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=589873 {ECO:0000313|EMBL:AIF99290.1, ECO:0000313|Proteomes:UP000056090};
RN [1] {ECO:0000313|EMBL:AIF99290.1, ECO:0000313|Proteomes:UP000056090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H 17 {ECO:0000313|EMBL:AIF99290.1,
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP008849; AIF99290.1; -; Genomic_DNA.
DR RefSeq; WP_044057393.1; NZ_CP008849.1.
DR AlphaFoldDB; A0A075P2V3; -.
DR GeneID; 78255561; -.
DR KEGG; aal:EP13_11680; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR Proteomes; UP000056090; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 1.20.120.960; Histidine kinase NarX, sensor domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal 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; IPR029095; NarX-like_N.
DR InterPro; IPR042295; NarX-like_N_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13675; PilJ; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000056090};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 227..445
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 460..575
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 593..708
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 508
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 642
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 713 AA; 78942 MW; 73834D5D217F3801 CRC64;
MSIRFRYIVA LTLIACLVTL SFFSMTGLFS SQRNDAEVIN IAGQQRMLSQ RIALISAHPS
FCDSSASTQQ MLASTLDTFI SNHTRLTQLT SLPKQVEQLY FSPGNLDTEV KQYIQQAQSR
LTQVNCMQPT SPFTLDQVSN LLAKLNEVVY QFELHAKRRV DKVANIELFL WLGTLVLLLL
EATFIFSPMR KAIESTIASL KQSHLEAKTA MDEAKAASQA KSDFLSSMSH ELRTPMNGLF
GMIELALDTP EKSESYLKKA KAAGRQLLSL INDILDLSKI EAGKIKVEKS PVDLLQLMDD
VVTIQRVYCV NKGLTFNYCK SATLPHIIEG DSTRIAQILH NLLSNAIKFT ESGAVSLAVN
ETHIDDKPTI VFTVTDTGIG IADEKLSAIF QKFEQADQST TRLYGGTGLG LSIAKRLAVL
MEGDISVSST LGKGSEFTVS LPLIEANLPP LEVNEVASLR CAVVDDLQTS REYLQHVLTA
MAIQPTTFAS ADAFLDDHPE QFDLLIVDLA MPNKSGVDLL REMAHLNIYP FPRVMLISAE
LELLDCEQEI RRLIWKTHAK PINRRELEAD LTKLINNDTP DNTAQRSKAQ KMRVLIAEDN
DINSEIVKAM LEAEGFKTLH VKDGEQAVAA CSKHKFDFIL MDCNMPVMDG IMASNIIRNE
LKVSTPIAAL TANVFPEDKE ECLKAGMNDF LTKPLNKGAL LASIRLHTQS DVG
//