ID S6IF12_9PSED Unreviewed; 929 AA.
AC S6IF12;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CFII64_20483 {ECO:0000313|EMBL:EPJ79633.1};
OS Pseudomonas sp. CFII64.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=911242 {ECO:0000313|EMBL:EPJ79633.1, ECO:0000313|Proteomes:UP000014850};
RN [1] {ECO:0000313|EMBL:EPJ79633.1, ECO:0000313|Proteomes:UP000014850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFII64 {ECO:0000313|EMBL:EPJ79633.1,
RC ECO:0000313|Proteomes:UP000014850};
RA Feris K.P., Lalor S.J.;
RL Submitted (NOV-2010) 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 -!- 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:EPJ79633.1}.
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DR EMBL; ATLO01000043; EPJ79633.1; -; Genomic_DNA.
DR RefSeq; WP_020292695.1; NZ_ATLO01000043.1.
DR AlphaFoldDB; S6IF12; -.
DR PATRIC; fig|911242.4.peg.4079; -.
DR OrthoDB; 9797243at2; -.
DR Proteomes; UP000014850; 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; 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; IPR036259; MFS_trans_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 SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EPJ79633.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:EPJ79633.1};
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..929
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004539614"
FT TRANSMEM 172..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 290..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 321..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 350..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 404..624
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 642..764
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 791..910
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 696
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 840
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 929 AA; 102944 MW; FFC54FBD8425106E CRC64;
MRWLRIAKRL TVGVLTLLFM LTAQAEQSAG WSTLLDSPAD LQLSDIRSAR FENAFSPIDL
AHITAADRNS ALWLHYRLQP NKHEQLLRIF APDLASLDMY VLNGEQMVDH SRTGNNIPRQ
DQLLHSRDFM LPLPQSDVPL DLYLRLVSTQ QLRPNITLQP AIESAADERE PFVLGLLLGS
LAMLILQNLT RYAHTRSPSN LWLAACEALL ALSAILLLNL LTPWLNTWHI PQTPSAHLTL
LLAAITGLMY TYCFFYHRKV VKLDRWLLGS LLVIALGALL ILFVDTLPLN LLTFGLVSLA
TLSILFVSAY NWQKGYSPAR LFVFSMITFN IGCLIILPAL LWLTMISPQW LIFTLLGVFC
VSGLLMSIAL SERHRSITED KFSISRDQAA STAEINAKAE FLAKISHEIR TPMNGVLGMT
ELLLGTPLSV KQRDYVQTVH SAGNELLTLI NEILDITKLE SGQIELDDVQ FDLSALIEDC
MNIFRAKAEQ QNVELISLIQ PQVPRVISGD PTRLRQTVLS LLENALKKTD EGEILVVVAL
DSRAGKPRLR IAVQDSGEPL APSERDALLH AELHSKNFLA ASKLGGHLGL VIARQLILLM
DGEFGIQTGS SQGSTLWLSL PLDADRLEQP PLDMDSPLKD ARVLVVDDND TCRKVLVQQC
TAWGLNVSAV PSGKEALALL RTKAHLRDYF DVVLLDQNMP GMTGMQLAAK IKEDPSLNHD
ILLIMLTGIS NAPSKIVARN AGVKRILAKP VAGYTLKTTL ADELTQRNKG AGPLPIAPVL
NTPINVPSDF RILVAEDNSI STKVIRGMLG KLNLHPDTAS NGEEALRAMK AQRYDLVLMD
CEMPILDGFS ATEQLRAWEV GNQRVRTPVV ALTAHILTEH KDRARQAGMD GHMSKPVELS
QLRELVEFWV AQRAKTHALT SDSDLYQQN
//
