ID A0A2T5P783_9PSED Unreviewed; 1231 AA.
AC A0A2T5P783;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DBO85_14900 {ECO:0000313|EMBL:PTU73600.1};
OS Pseudomonas mangrovi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=2161748 {ECO:0000313|EMBL:PTU73600.1, ECO:0000313|Proteomes:UP000244064};
RN [1] {ECO:0000313|EMBL:PTU73600.1, ECO:0000313|Proteomes:UP000244064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC-11 {ECO:0000313|EMBL:PTU73600.1,
RC ECO:0000313|Proteomes:UP000244064};
RA Chen C.;
RT "Pseudomonas sp. nov., isolated from mangrove soil.";
RL Submitted (APR-2018) 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 -!- 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:PTU73600.1}.
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DR EMBL; QASN01000020; PTU73600.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T5P783; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000244064; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 3.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
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; IPR005330; MHYT_dom.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
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 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; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF03707; MHYT; 3.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50924; MHYT; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:PTU73600.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00244};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000244064};
KW Transferase {ECO:0000313|EMBL:PTU73600.1};
KW Transmembrane {ECO:0000256|PROSITE-ProRule:PRU00244};
KW Transmembrane helix {ECO:0000256|PROSITE-ProRule:PRU00244};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 24..47
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 59..85
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 97..115
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 124..145
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 157..176
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT DOMAIN 22..215
FT /note="MHYT"
FT /evidence="ECO:0000259|PROSITE:PS50924"
FT DOMAIN 266..336
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 341..393
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 394..468
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 471..523
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 538..564
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 593..645
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 663..879
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 902..1021
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1051..1151
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 951
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1090
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1231 AA; 134193 MW; 544D379880D24211 CRC64;
MQGLSSFFLL SASPEQLLIG EYRPWLVALS VLVAVLTSAM ALQLAGVARR AASAFYRQLA
IATGALALGG GVWSMHFIGM LAFAICAEVV YDPALTLLSV LPSLAASWVA LNLLARKQVS
HRQLLLGGSL VGAGIGTMHY AGMAAMSMAP LLRYDPWLFG LSLLVAVALA TGALWIRFGL
RGRVPGHLAL LLGSLVMGSA ISGMHYVGMA GARFVGLAES ATPLPVYGSA YLALAVAMAT
LSFSVLVAAA NGLLRYRQLA TELEEGRLHL DSLLDAAREV ILTVDHQGIV RSANRSAQRL
YGWPPDELVG QHMSVLMNEQ HRETFGQALQ NYMRSGRPQL SGIELELNGR ARDGREIPVR
VSLGVSHREG KPWFVVFVAD IAERKAMEQA LRESEQQYRS LIGNIPGVSF RCLLDADWSM
LFISDAVEQL TGWKPADFTE RRCSFADLYH PDDLARVAED VQRAIAERRN YQVEYRIRDR
QGREHWIWES GSAVCDENGV PHWIDGVLLD QTDSKLRNAE YESKVNAISR AMVMVEFDMQ
GRILALNDNF IELFGYQREV LLGQHHSLLC APEEVAGSDH QRFWDDLRQG LFRAGECQRF
AHDGREIWVQ ASYNPILDAD GKPFKVLKLA TDLTPRRMME QELRAARDRA EQAAAARSSF
LANMSHEIRT PMNAIIGFTD LLLDAAAEPT QRHQLSIVQQ SSRSLLRLLN DILDTAKLDR
GAIELETLDF SLRELCRQVC DALRLGAEQK GLVLEMGFTE RVGDIYRGDP LRLRQVLTNL
LGNAIKFTEQ GRVGLQVSGE PGALRLIVSD TGIGIAEDRL EKIFDPFAQA DASMSRRFGG
TGLGTTISRQ LVELMGGRIQ VRSRLGEGSE FIVELPLAAG SAVTGAEPGL APVATPGLPP
LRILAADDVA QNLELLALNL EPLGHRLVKV SDGAAATEMF ARETFDLVLM DVQMPGTDGL
EACRRIRALE AAEQRKAVPV IALTASVLDR DRQAALDAGM NGFASKPLEM PALLGEMARL
LGLEQAPAQA TGAAGAGSLF DWRGGGRRWG SPLRMADAVK RFLDDEAGLA TALLSALHAA
EWQQVQQQAH RLRGAAANLG LRQLALLGEA LECAASAQDN RRVEQLCAEL PRTLTAIAVA
VPLAPVSVQP PAQPLDLPSL REACAQLQLQ LRRGALDDAA VACLEQALVD RQPEALDRLR
SALQGFDFDL AQQAVADLQA WLDNPSEERA E
//
