ID A0A1I1I885_9GAMM Unreviewed; 977 AA.
AC A0A1I1I885;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN02745724_01425 {ECO:0000313|EMBL:SFC32386.1};
OS Pseudoalteromonas denitrificans DSM 6059.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1123010 {ECO:0000313|EMBL:SFC32386.1, ECO:0000313|Proteomes:UP000198862};
RN [1] {ECO:0000313|EMBL:SFC32386.1, ECO:0000313|Proteomes:UP000198862}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6059 {ECO:0000313|EMBL:SFC32386.1,
RC ECO:0000313|Proteomes:UP000198862};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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: 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOLO01000007; SFC32386.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1I885; -.
DR STRING; 1123010.SAMN02745724_01425; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000198862; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
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 InterPro; IPR007892; CHASE4.
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; 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 PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF05228; CHASE4; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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; 2.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
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 Kinase {ECO:0000313|EMBL:SFC32386.1};
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:UP000198862};
KW Transferase {ECO:0000313|EMBL:SFC32386.1};
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..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 343..564
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 580..689
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 713..829
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 881..977
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 627
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 762
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 920
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 977 AA; 110549 MW; CF164091F8F0440B CRC64;
MLFNKLGWLT LICWLLLIIS ILLLLPYGIQ KWIVLPSFLK LEQEFAQKDL IRVIDAIKRE
VHHLEAITTT FASWDETYEF ITTSNDRYIK TSFSVGSFIS ADIHMYHIYN NEGVLLKGEI
YDTEYKKKIK VEQFSAPKLE NNNIYLLKHK NFSLLGIINT QAGLMAINAR PILTSQGEGP
VMGTVVMGRF LTKKFFNSLS KQTKVEFSVI PLNRSTLALQ NFNDALYILN DKTAIKAINT
DFIEMYGIID DIYNEPVLLT HLRIPRDIMV HGKHAAKLTS ISIISSLFVI SASLFLFFIK
YSMDIRQNNK LIKIKVAQRT EELVQAKDEA IKANRAKGDF LANMSHELRT PMNAILGMAE
LCQQTELTMK QQKFVGNIHY SAKSLLHLFN SILDFSKIDA GKVELEFVDF TLDDILCPLE
VLTNEQVRAK DIPLIFDIKL NLSYMIIGDK LRLRQIMLNF IQNSLKFTES GSIYLKVRLV
DEVDDWVWFE FLIQDTGIGM DPETIAHIFD EFSQADTSTT RKYGGTGLGL SICKQLIELM
GGEVSLDSEL GKGTQVKIRM PFQLSSQENV GFFEALVGHK ILIYSEDQAY AHALLNTLSR
YGSRVTLVDS AEKALSFAST HDTCLIDDAL PEFDIINFLT SLNLQAKLLD TILLTNNTEP
KEVYTIFNLS LLTKAVYLNN FIQASKLLST EIKSFKLSHD KLDKLFHSLH DKNILLVEDN
DINQQVIIEL LAGIGIATIC AENGEVALSL LENSQFDAIL MDIQMPVMDG IETTKVIRSN
MLWQDIPIIA LTASAMVGDK EKSLAIGMND YLTKPIFPEQ LYDCLERWCS HSKVNTSTKE
PVNPINDKVI NEGHENNDNE IQIQKDDVLD ITAGLKVCAG KRHLLESMWK RFVEKHSDSG
KKLQAYLSSH EYEKALALLH NLKGVSGNIG ALQLYTEVTQ LHTLLAQDET QLNEHDIKKV
IIGLSKVCDC INKQINI
//
