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Database: UniProt
Entry: A0A095X0I4_9GAMM
LinkDB: A0A095X0I4_9GAMM
Original site: A0A095X0I4_9GAMM 
ID   A0A095X0I4_9GAMM        Unreviewed;      1804 AA.
AC   A0A095X0I4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=HRUBRA_00993 {ECO:0000313|EMBL:KGE04409.1};
OS   Pseudohaliea rubra DSM 19751.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC   Pseudohaliea.
OX   NCBI_TaxID=1265313 {ECO:0000313|EMBL:KGE04409.1, ECO:0000313|Proteomes:UP000029640};
RN   [1] {ECO:0000313|EMBL:KGE04409.1, ECO:0000313|Proteomes:UP000029640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19751 {ECO:0000313|EMBL:KGE04409.1,
RC   ECO:0000313|Proteomes:UP000029640};
RX   PubMed=25414506;
RA   Spring S., Fiebig A., Riedel T., Goker M., Klenk H.P.;
RT   "Genome Sequence of Gammaproteobacterial Pseudohaliea rubra Type Strain DSM
RT   19751, Isolated from Coastal Seawater of the Mediterranean Sea.";
RL   Genome Announc. 2:e01208-14(2014).
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: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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:KGE04409.1}.
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DR   EMBL; AUVB01000027; KGE04409.1; -; Genomic_DNA.
DR   RefSeq; WP_052094836.1; NZ_KN234785.1.
DR   STRING; 1265313.HRUBRA_00993; -.
DR   eggNOG; COG0642; Bacteria.
DR   eggNOG; COG0834; Bacteria.
DR   eggNOG; COG4251; Bacteria.
DR   HOGENOM; CLU_238021_0_0_6; -.
DR   Proteomes; UP000029640; 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; 3.
DR   CDD; cd01007; PBP2_BvgS_HisK_like; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
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; 3.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 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; IPR036641; HPT_dom_sf.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR013655; PAS_fold_3.
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   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   NCBIfam; TIGR00229; sensory_box; 3.
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; PF01627; Hpt; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 3.
DR   SMART; SM00091; PAS; 2.
DR   SMART; SM00062; PBPb; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
DR   PROSITE; PS50113; PAC; 3.
DR   PROSITE; PS50112; PAS; 3.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000029640};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        294..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        337..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        633..655
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          672..718
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          743..797
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          798..843
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          874..926
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          956..1011
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          1016..1069
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          1087..1309
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1326..1445
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1469..1585
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1623..1724
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   COILED          910..937
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         1377
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1518
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1662
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   1804 AA;  196198 MW;  1C2354135E7599D6 CRC64;
     MPRLARWHYL AVTGLLAGLL IASFLFQGAP QAQGDRSGPV RLELTEAERQ WLREHPVLRA
     SGETDWPPFN FRYADRQHGY SVDYLELLAK RLGVEVEYVT GRSWSQFMED LREGRVDVLL
     NAVRTEDRAR WMAFTNPYGD FTVGIASRGQ DPIRTSAALA GRTVAHAAGF ASEQFLADYI
     PEADAVPAAD IRAALDLVAA GKADAAIGVT PSMRYQIAEH LLDNVAVTGI IPVPGDDWRL
     LRLAVHKDQQ QLVTILEKAV ATVSERELRS LRAHWLDDAQ FRGAIAAGED EPSLGFLAPS
     LVALVLVLLI ALLWLFFNRL SAPMQERLVS DARLRAWLVA LLLAFFLVTT WLAWHAMERR
     ELATRKLYGE TLLGINALLL EDLRQWSARW RDVARQLAAD PRVRATVMEG EPAAMEKSCR
     LLGAVCAFAG RDDLRVVLAG GETVAQLSVP EAVWQGDTRF EVLPPRPGEP RRFAVFAPVR
     DGPDEAISGA VILTKSLVEA GLLRVFEAAR VGGTGESYAM DGTGRLVSAT RFPGMVQGFA
     KLLEDGVLQA RDPGGSLQDG YEPTGKPSQW PLTRLAQSAL AGDTGVDIDG YRDYRGVTVF
     GAWAWFEPLG IAIATEIDAA EVLDPLRLEQ KRLIGLLSAI LLVVLALLAF LFWLGGTARL
     SLRRRLQQQE RELRTLGAAL RASPLAVLST DREGTILSTN PAFTTITGYT PEEALGQTPR
     ILKSPRTPTR THDELWDSLL AGNTWRGELV NRCKDGSEYN ARMTITPLLD NRGQPETFVG
     VQEDITETVS AHNAEARASR RVELLLANAG EGIVGLDRQG HIVFTNHALR TMLGYDAGEL
     EGEYMHGKLH YARVDGSPMP ESECHMMPGL EARQVVEEDV LWRRDGTPLS IAYTASPVQD
     DPDGLAVVVV VRDITARKRA ERQLQSAEQR LVGAAEAAGL GLWEYRPGQG VRDVSVNEQL
     PRLLGYAPEQ LRAGSGPWAP LREGHKTMEE LLNPEDVPSV GEHLMNMLRA RGEYTSRVEF
     RMRCADGRWR WFAAVGQVLE RDAEGRALRV AGVQIDIERD KELAHRLEEA KLAAEAASRA
     KADFLANMSH EIRTPMNAII GMTQLALNTE LNERQRGYVG KSYEAAQSLL TIINDILDFS
     RIEAGRLEME SSEFDLDEVF GGLGSLVGLS AEEKGQELVF YRAPNVPRWL VGDAGRLRQV
     LVNLGSNAVK FTGDGGEVVV MVQLAAASDD IAELHFSVRD TGIGMSEEQQ QKLFQAFTQA
     DTTITRRYGG TGLGLAISKN LVGLMGGRIW CESEPGIGST FHFTAQFIIA GEDGAALPGA
     EVDSPRVLLV EDSATTRMLV ASMLSNLDCE VDSVDSGEAA LIRLAAADRP YDVVVMDWKM
     PGMDGIATVR AMLDDDRFAD VPAVVMATAY AANDARSAAG DLPIEIFLQK PVTPSSLFDA
     IVTSLGAHVV SAGGARPRNP GSSGITGARI LLVEDNDINR EVAQEFLAGE GVEVLTAVNG
     EEALAVLEQE AVDGVLMDCQ MPIMDGYEAT RKLREQPAFA ELPVIAMTAE VMTGDRERAF
     AAGMNEHVGK PIDFDELSAV LRRWIVPASG RAAPRRPVPS MVPELPLLPG IDRDAALANA
     GGSGELVLRL LDRFRKDYRD YEGSFREALR VEDGAAAERS AHTLKSVAGT LGAGDLETAA
     GDLERTLKEN GDQGSVDEAL ASTLAALAVV LESLEALHEA GPAERDASDQ AAPDSEALAN
     GLAELDRLLA DNDTGALELF AHLRDALEAR YGERPIRRLA VAVDGYEFGQ ARTRLAALEP
     GDAA
//
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