ID A0A077LJZ5_9PSED Unreviewed; 930 AA.
AC A0A077LJZ5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PSCI_2421 {ECO:0000313|EMBL:BAP43123.1};
OS Pseudomonas sp. StFLB209.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1028989 {ECO:0000313|EMBL:BAP43123.1, ECO:0000313|Proteomes:UP000031652};
RN [1] {ECO:0000313|EMBL:BAP43123.1, ECO:0000313|Proteomes:UP000031652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StFLB209 {ECO:0000313|EMBL:BAP43123.1,
RC ECO:0000313|Proteomes:UP000031652};
RX PubMed=25323715; DOI=10.1128/genomeA.01037-14;
RA Morohoshi T., Kato T., Someya N., Ikeda T.;
RT "Complete Genome Sequence of N-Acylhomoserine Lactone-Producing Pseudomonas
RT sp. Strain StFLB209, Isolated from Potato Phyllosphere.";
RL Genome Announc. 2:e01037-e01014(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};
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DR EMBL; AP014637; BAP43123.1; -; Genomic_DNA.
DR RefSeq; WP_045486958.1; NZ_AP014637.1.
DR AlphaFoldDB; A0A077LJZ5; -.
DR STRING; 1028989.PSCI_2421; -.
DR KEGG; pses:PSCI_2421; -.
DR HOGENOM; CLU_000445_105_0_6; -.
DR OrthoDB; 9797243at2; -.
DR Proteomes; UP000031652; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.60.40.2380; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
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; 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; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF07696; 7TMR-DISMED2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 2.
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 Kinase {ECO:0000313|EMBL:BAP43123.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000031652};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:BAP43123.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..930
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001720349"
FT TRANSMEM 172..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 233..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 266..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 321..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 403..623
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 641..763
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 792..911
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 695
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 841
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 930 AA; 102917 MW; 62B2C9B1742BB6AC CRC64;
MRWLRIAIAS TASLLTLFFM LSAHAAATTG WSTLLDEKGH LSIAEVRAAH QQNQFSPREL
DSITAAKRDG AVWLHYRLTP EPHEQLLRIF APDLASADLY VFQGDRQIDL LRTGNLIAKQ
NQRLPANDFL LPVPQAQTPL DLYLRMVSSQ QMRPNITLQP AIESAADERE PFLFGLVFGL
LAMLILQNLA RYSHTRSRTN LWLAACETLL ALSALLLLNL LDLFDDWHLP QTPGAHVALL
LAAVTGLMYT YCFFAHRKSR AVDRLLLIDG SLMVIGTLLV LLVDDLSINL VTFVLVALTT
VSILGISVLH WIKGYRPARL FMFSMIIFNL GYMVVLPGLL WLSLIPPQWL ILTLLAVFCV
SGLLMNTALG ERQRNIVESK FSISRDEAAS TAEINAKAEF LAKISHEIRT PMNGVLGMTE
LLLGTPLSVK QRDYVQTIHS AGNELLTLIN EILDITKLES GQIELDDVQF DISALIEDCL
NIFRAKAEQQ NVELISLVQS QVPRVISGDP TRLRQTLLSL LENALKKTEG GEILLVAALD
NRGGKPRLRI AVQDTGEPLS GEERDALLHT ELHSKNFLAS SKLGGHLGLV IARQLIILMD
GEFGIQNSTG QGNTLWLCLP LPAHLLEQPT LDLDGPLKDA RVLVVDDNDT CRKVLVQQCS
AWGLNVSAVA SGKEALAMLR TKAHLRDYFD VVLLDQNMPG MTGMQLATKI KEDPSLNHDI
LLIMLTGISN APSKIIARNA GIKRILAKPV AGYTLKTTLA DELTQRSKGT AYVAPSALPL
AAAPIDVPGD FRILVAEDNN ISTKVIRGML GKLNLKPDTA SNGEEALRAM KAQRYDLVLM
DCEMPVLDGF SATEQLRAWE MGNQRVRTPI VALTAHILTE HKDRARQAGM DGHMAKPVEL
SQLRELVEYW LAQRDRTRAK TTEEKVYQQN
//
