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Database: UniProt
Entry: A0A075P2V3_9ALTE
LinkDB: A0A075P2V3_9ALTE
Original site: A0A075P2V3_9ALTE 
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
//
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