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Database: UniProt
Entry: A0A0P1H0X1_9RHOB
LinkDB: A0A0P1H0X1_9RHOB
Original site: A0A0P1H0X1_9RHOB 
ID   A0A0P1H0X1_9RHOB        Unreviewed;       909 AA.
AC   A0A0P1H0X1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=luxQ_3 {ECO:0000313|EMBL:CUH83703.1};
GN   ORFNames=TM5383_00903 {ECO:0000313|EMBL:CUH83703.1};
OS   Thalassovita mediterranea.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Thalassovita.
OX   NCBI_TaxID=340021 {ECO:0000313|EMBL:CUH83703.1, ECO:0000313|Proteomes:UP000051681};
RN   [1] {ECO:0000313|EMBL:CUH83703.1, ECO:0000313|Proteomes:UP000051681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8383 {ECO:0000313|EMBL:CUH83703.1,
RC   ECO:0000313|Proteomes:UP000051681};
RG   Swine Surveillance;
RL   Submitted (SEP-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};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CYSF01000006; CUH83703.1; -; Genomic_DNA.
DR   RefSeq; WP_058317846.1; NZ_FTNX01000001.1.
DR   AlphaFoldDB; A0A0P1H0X1; -.
DR   STRING; 340021.TM5383_00903; -.
DR   OrthoDB; 9801651at2; -.
DR   Proteomes; UP000051681; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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; 1.20.120.160; HPT 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; IPR036641; HPT_dom_sf.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 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; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000313|EMBL:CUH83703.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000051681};
KW   Transferase {ECO:0000313|EMBL:CUH83703.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        227..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          265..336
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          412..630
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          657..774
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         706
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   909 AA;  100549 MW;  B12086554D5C10D7 CRC64;
     MPIEPHTDSI ETPPKRGIAR LWGAVSKRFA RAHAPFTGQQ FSDEELYAVH PTSTQRVIGN
     PRLLALLSVV GFIVMTTLTM QVVRDVRLLR QSTIEDIEWS LSKAEVEFLS YQYALRQAAH
     GRVDNFVTLR REFDILQNRI EDLRFGVIYE PLRDVPGFNA ALDSVSQHLG ASAPALRSVD
     ATLARSLIEV EEHALAMTPH VRAMAAAGQT NLEILFDRHQ MALSTTLQVM GAVGFILTAS
     LGLLAFYFNQ LRQQSDARRR SLITAGERTR AVMASSLDAV IVCDPEGVIE EFNAAAEEIF
     GHRREDAIGA NVADLIVPAE QREAHVRGMR RVSRGGGFHM VGKGRVRMEA RRADDTMFPI
     EMALQKSESH GHMMYIAFVR DISYRVRAER DLIEARDQAR AGEKAKSRFL AVMSHEIRTP
     MNGILGNMSL LRETKLSPEQ EGYLAHMESS SDILLGHVND VLDIARCEDG KPVVQYRPTR
     LRDIIDSAVE SMRPPAEDNG NSLTLIHSGP DLGWVQTDPG RVQQMLLNLL SNAAKFTENG
     SIIVDVRCKA QEDDITIHIK DDGIGIAEPD LDRVFEDFFT QDDSFARKTE GTGLGLGIVR
     RISEALGGSV SVTSKLGIGT TFTLRLPMPR CAAPEDVTPP EPKVSDAMEQ NTTDMLRILV
     VEDNQINRDV VRAMLTREGH LVEEAHNGQS GVEKASEKEF DLILMDISMP VLDGREATRA
     IRDGEGASAN SPIIALTAHV MPENVTEFLG LGMQDVLPKP LLRPDLQRII RDHAAAANND
     TCPTTVRMNQ MRQLVDMEVN KALRESVGEA YDMLLGQMSE ELQDLLEWLQ AAEQPLPEVA
     DRCHKFASSA AVFGALPLQK LLVGIELAAK SRDTVEVERR LAQLPEMLAT SLNHLQGGGM
     GHNQGRKRG
//
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