ID A0A0S2JXK7_9GAMM Unreviewed; 1423 AA.
AC A0A0S2JXK7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PP2015_345 {ECO:0000313|EMBL:ALO40871.1};
OS Pseudoalteromonas phenolica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=161398 {ECO:0000313|EMBL:ALO40871.1, ECO:0000313|Proteomes:UP000061457};
RN [1] {ECO:0000313|EMBL:ALO40871.1, ECO:0000313|Proteomes:UP000061457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 12086 {ECO:0000313|EMBL:ALO40871.1,
RC ECO:0000313|Proteomes:UP000061457};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-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; CP013187; ALO40871.1; -; Genomic_DNA.
DR RefSeq; WP_058028647.1; NZ_CP013187.1.
DR STRING; 161398.PP2015_345; -.
DR KEGG; pphe:PP2015_345; -.
DR PATRIC; fig|161398.10.peg.354; -.
DR OrthoDB; 9782200at2; -.
DR Proteomes; UP000061457; Chromosome I.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; 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; 3.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 2.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF13426; PAS_9; 2.
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; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 3.
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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ALO40871.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000061457};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 230..273
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 286..340
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 576..627
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 628..701
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 705..758
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 759..831
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 834..886
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 904..1125
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1142..1261
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1301..1422
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1194
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1352
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1423 AA; 160889 MW; C75F40778376CB51 CRC64;
MLSTESFIAT FSRRYKIALI VIALAITTTF FILNEQQIKQ KDSAHIINIA GEQRMLSQRL
ALLVQLSYKT QSQKNSQKLK QVAERLLENQ GFLLKKVSSK DASAQAELSK HFQDTRLLKR
LEQYTGLAIE NSQSYSPETL QQFEQFDNEQ LLIDLDHTVK LFEKATLAQQ LTLQRINLAL
WAISLLVILF LVFAIFKPTQ RWLSDTYQRL LLEKNRVKDV QFAINKHSVV MRVDSDTNLL
FYNKKFSEHY GYEQDELIGQ PVKVLRSGIH DDSFYDTLNQ AIQQRKVWQG EICNRAKDGR
LYWFDTSIVP IKHFENEAES SIVIQNDITE QKRTLGALTQ IHVITSDSNA SLDDKINKLL
VLGRQIFNLP LAIISNINEE KNTYLVKYAS TPNDAINPGD IFDYKNSYCI HTLKANHAIA
YHHVGQSDIA HHPCYESFAL ESYIGCPLII SGRRVGTLNF SSPEVSPHEF SDTDLEIVQL
LAHWISHEFT REEQENKLLL QQQLMNQMSE QANIGAWEVD LVSEKVYWSD MTKQIHEVDS
DFEPQLSTAI NFYKPGFSQE RISELVAQSM QTGEPYQEEL QIITAKGNEV WVEAKGQTEF
RDGLCIRMFG SFQDITERVE AQNKLKFSNQ RLEFVLDSTG VGIWDWEIDS GITTYNERWA
NILGYKLKEL EPTNTLTWVD LVHPEDFKYS EHALREHWNR ENEIYLCEIR MKHKLGHWVW
ILDTGRVVEW NIDGSPKRMI GTHLDISASK KAEQEIQDKN ERMALAADSA GIGIFDYNLE
DDSLSWDNWM FKLYGIPESD FSAAYNAWEQ SLHPDDKEKT EALLSDAIKH DSKFDTQFRI
ILPNGQIRHI KASAINKVNE HGLVTNVVGV NYDVTERVQY EQALQQAKTV AETAVVAKNE
FLASMSHEIR TPMNGVIGML DLLTSSELSD EQQHRVSIAQ SSANSLLTLI NDILDFSKID
ADKLELENIP FNLTTMLGEL CESFAMTIEA KGLELILDTT ELPNQLIISD PGRIRQILTN
LIGNAIKFTH TGEILISAHL QGTDLDSLDL ILKVKDTGIG IAQDKQAHVF ETFSQADSST
TRNYGGTGLG LAIVKKLCNR MNGSISLQSS LGEGSEFTCL LKVSSCEKNH TKVPDVDISS
LNILVVDDNE TNREILDKQL SQWGAKVTTS HNGEHALTVC KSQTEAMFDI AILDMQMPNM
DGAQLAQHLQ SIPECEQMQL IMMTSMQTRG DAKYFADLGF KGYFPKPTTT QDLLGALKII
SDKGDSLENA KPLVTHHYIN ELQQADENPE LNDNKPLPSL NILLVEDNPV NQIVAKGVLK
NLGQACDSAD NGQQAITQLK SCDTPYDVIL MDVQMPEMDG FQATQLIRQG KAGAHHQNTV
IIAMTANAMK GDKEKCLDAG MDEYIAKPIS LNALREKLLQ STS
//
