ID F9UBN1_9GAMM Unreviewed; 1717 AA.
AC F9UBN1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ThimaDRAFT_2333 {ECO:0000313|EMBL:EGV18349.1};
OS Thiocapsa marina 5811.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiocapsa.
OX NCBI_TaxID=768671 {ECO:0000313|EMBL:EGV18349.1, ECO:0000313|Proteomes:UP000005459};
RN [1] {ECO:0000313|EMBL:EGV18349.1, ECO:0000313|Proteomes:UP000005459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5811 {ECO:0000313|EMBL:EGV18349.1,
RC ECO:0000313|Proteomes:UP000005459};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Cheng J.-F., Goodwin L., Pitluck S., Peters L.,
RA Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V., Frigaard N.-U.,
RA Bryant D., Woyke T.J.;
RT "The draft genome of Thiocapsa marina 5811.";
RL Submitted (JUN-2011) 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; AFWV01000007; EGV18349.1; -; Genomic_DNA.
DR RefSeq; WP_007193208.1; NZ_AFWV01000007.1.
DR STRING; 768671.ThimaDRAFT_2333; -.
DR PATRIC; fig|768671.3.peg.2471; -.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG4564; Bacteria.
DR OrthoDB; 5555106at2; -.
DR Proteomes; UP000005459; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.450.350; CHASE domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR004010; Double_Cache_2.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR033480; sCache_2.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF08269; dCache_2; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01049; Cache_2; 1.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 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; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EGV18349.1};
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:UP000005459};
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 16..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..391
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 663..684
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 435..591
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 697..767
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1195..1416
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1433..1558
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1582..1696
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 872..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1487
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1631
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1717 AA; 188155 MW; 8DCB31457DED6B34 CRC64;
MLRQAIAAPD PGSPRLLIRA AIALAVLVLI GGSLGAWWSV GLADREMKDS LLLDTRLLAQ
SLNVERVAAL TGGPADLEKP EYERLKSQLA IVAKTDPRYR FVYLMGRRAD GQLFIFVDNE
PPDSDDYSPP GDPYDEASEG ERRVFATGDE HVEGPLVDRW GTWVSAQVPI FEPSKAVGGS
ALPAEARALV QNAAAYAEQH GREALLEALR EPNGPFHRGD LYAFAYDLDM TFLAHPAKPD
LVGKNLIDRP DRVGGTLFRR EIQRIALSQG SGWVAYEYEN PINDRVEPKT TFVQRVGDMI
VCAGAYRVQG GVVAVLGIDV EAVTWKVALA KTAVPTLVLT GVLLLIILAG TALLVRRTRL
EPHAAQRWRH LEPMLVMAAG LALTLFAAWM AHQREGHARD WSFAQLASAR TEAIAETLQN
LRDTELQGLA SFVESSAEIT AADFERYTTY LTRNPAVRAW GWAPRVDATD LDDFGARAKA
AGIEDAQIWQ EDARTGRVPA AARESHYPVL FAAPSTRANL QALGFDLASD PQRRAAIDAA
TLGDLPTATG PITFVLEPGS PKGIRVVQPV RGDSRDVRGV VAAALRMDTL LLGDGPDKAT
RLQVAYLHPS GHFEPLASNW NPNGEQPGGP SLTRLLPIFG KVFAVTASAG PEFLSRHPAR
AGWITALTGF ALTVACVLVA TLLARRHAGL VGLVNARTEE LNRFFTTGLD MFCIVNAEGV
FLRVNPEWER TLGYPPEELE GQAFIDFVHP QDREATREAT RRLDAHGAIL DFENRYRCRD
GSYRWIEWRS FPSGELIYAA ARDVTERKRA QAETARRLEL ESAAAAISAR FARARPDNFD
AILDQALQKL GELLEVERAY LFRVSEDGSR MTNTHEWCAP GTPSRMERSQ DQPVDQLPWW
KARMATGEPL LIPGVAALPD DAGAEKAEFL TRGIGSLLCL PMVASGGTLG GFVGFDALHP
RHAWAKSDIG LLQLLVQVIG STIKRLDTFA HLQDSEKALQ RETRLQGLLM EISSTYISLP
LDRVDSVIET SLGHLGDFVG ADRAYIFDYV FERQIVTNTH EWCGSGIEPQ IDTLQAVPME
MIPDWIATHR EGGTVYVPDV LSLAPESSVR QVLEPQGIKS AIAVPMIDGP RCRGFVGFDS
VRRHHRYSDT EQRLLTVFAQ MLVNVQKRRE TEDSLRLSRE QAEAASRSKS EFLANMSHEI
RTPMNAVIGL SQILLGTDLN DEQRDYLGKI HGSSRLLLGI INDILDYSKI EAGKLDLESR
PFRMDELLDQ MATLFGSAAG EKGLELVFRV SPDVPRTLLG DALRLGQVLT NLLANALKFT
EQGTVEIRIA RLGGDTAQVK LRFEVADTGI GMDTEQIDRL FQAFSQADSS TTRKYGGTGL
GLVISRKLVE RMGGRLTVAS APEAGSVFSF DLLLPVSRED SEPRDLRKIA GARVLVVDDH
AVSRTVLREI LQSWRCRVDE AASGAAAVQA VIEAERAGRP FDFILMDWKM PGDLDGLEAT
RQLFRLRKEG RLTGAETPAI IVSGYNRDDL PKERSGLSGF LGKPVTASAL LDTLLEAHGE
KPHPGRTAPT ARAPIPSFTG AAILLVEDNA LNQEVAKRML QRTGAVVTLA ENGIEAVALA
TTQDFDLVLM DLQMPMMDGF EATRRIRPQR PDLPIIALSA AVMEIDRNGA REAGMNGHLA
KPIDTVELYR TLALWLPGHD DGEPQGTGAR RTDQASD
//
