ID S6GQY0_9GAMM Unreviewed; 2224 AA.
AC S6GQY0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=OFPI_23390 {ECO:0000313|EMBL:EPJ49665.1};
OS Osedax symbiont Rs2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae.
OX NCBI_TaxID=1330035 {ECO:0000313|EMBL:EPJ49665.1, ECO:0000313|Proteomes:UP000014830};
RN [1] {ECO:0000313|EMBL:EPJ49665.1, ECO:0000313|Proteomes:UP000014830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rs2 {ECO:0000313|Proteomes:UP000014830};
RA Yi H., Goffredi S.;
RT "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT Osedax worms: functional variation and environmental selection.";
RL Submitted (MAY-2013) 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:EPJ49665.1}.
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DR EMBL; ASZI01000179; EPJ49665.1; -; Genomic_DNA.
DR PATRIC; fig|1330035.3.peg.2240; -.
DR Proteomes; UP000014830; Unassembled WGS sequence.
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; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 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 Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
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; PTHR43642; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR PANTHER; PTHR43642:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SMART; SM00220; S_TKc; 1.
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; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000014830};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..266
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1497..1718
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1736..1857
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1881..1997
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 2043..2135
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 1790
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1930
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 2082
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 2224 AA; 250540 MW; B1DD01AC44F6B6BC CRC64;
MIADFTVTKI LTSSDSVHYA EALDEQQQPC LIKYVNSAAH MNYTSAELKL EYNLSRSLNS
AWLLPTKELL EDPQHTMIIY PAIPGQLLGA YIQDYQLTFA SKLRIAILLV EAVHYLHTNN
LLHRNICPEA FWLSKNEQRL YITDLSLVTK LEKDDSSNRS NQLIGNVAYI PPEQTGRSNL
AIDNRSDLYS LGASLYELFS GRQIFAEGDQ DSLSIMYKQL TQKVTPLDEV DQQIPKVISN
IVTCLLEKSP DKRYQSSFGL LSDLKIIADQ WRNSQRVSQF SIGTTDSPEK FNISKKLYGR
ESEVERLMQE FKSVSAGCSE LLLVGGYSGV GKTALVKELQ KPITANRGMF SLGKCDQFNA
DQPYFVFIQA LRLLMRQLLS LDTLTRDKWQ QHLQTQLGSN ISVLIELIPE LQTLFAETIS
PPETLSVLEN ENRFLLTLCQ FVAAFSKAGE PLVLFLDDLQ WADSASLKLV EKLLLQPNCL
MIIGAYRDNE VDATHLLMAT KQRIKASKIK LCELNLKPLS RIDIQHLIAD SLWLEPSAVK
PLATICSQKT QGNPFFINQF LLMLSEEGHI YYDYHMGQWD WYTEQIENMS ATSNVVELML
SKLIKLPADT IEIMKFAANL GSKFSMQKLQ IVSQLSLQQA YQHLWPMIKQ GFILPLDEHY
RFESDEKLLA QAKFAFLHDK VQQAAYQMIS PAELSDFKWQ AGNRLLNATV SEELDTRIFE
IVEQLNAGIG AADSTELQQL VQLNIQAADK AKRSSAFGSA RQLLHNAYLL EESASKAQRL
TIYLSLAEMS YMTGDFDFAQ SLYPKAMQVT ESALQKVSVY ATQTAQYQIQ GRFIEAIEIQ
KMGLSALGIK IPDEQSLVFE RFMQGFENID LLIADQSISE LLNRQQMTDP QQDAAMHLLK
GMWYASYLSG QTSLNLLSSI LMTEMSLNYG HNDISPFAYV NYALAVIAVY QRYEQGDEFG
QLAITLADSR DNKLIRASTY FLYATFTHHW NKPLQLSVPF FERSYDLALQ SGDLATLGYI
CAVRASDSLA LGADLSQAEQ HLSREIELLQ KHRQQDMSDC VRVGALQSIK ALLGMTNNLQ
TFDDPQFNEQ DFLHDYSQAP LHLAYYYSAK IRHAYLTHDT REQQLALLNH SETVFAYVPG
QNKIPECGFY SALIMLRFAS DEADILYIQA QQYLQQLAGW SKYCQANYQH KYLLLRAESA
RVRSEYANAI ELYAQAIEQA KEYQYENILG VANECFAEFW RQQNKQEIAK SFIISAYAAF
AQWGAVAKLE QLQSQWFNVN FDAQITGTAQ QQPDQINLQT VQDLNQLISR ELDLEHLLEK
LMLILLKNAG ADWGCLVHVN QGSLLLEAAG DKDSILVLLN QHLSTAQAKK LLPESIIQYV
LDNPKLQVLN RPFEMTEYRQ DRYFETKQPL SVACIPVIHQ AKTIAIVYLE NQLTENAFGQ
RHISLLNVIA SQAAVSLSHA FLYQSLEKRV VQRTTQLAQA KLKAEQATFA KSNFLANMSH
EIRTPMNAVI GLSRLVQRTE LSIEQDDYVT KIIDASESLL SLINNILDFS KIEARKLAIE
EISFNLTDSF QRVINICGHK VHQKSLEFVI DIAADVPTAL IGDQLRLQQI LINLINNAIK
FTDSGSILVK VILSETEQSQ CELQFSITDT GIGISEQEQR QLFDSFYQGD ASSTRKYGGT
GLGLAISKEL TELMGGNIHV DSKLNQGTTF SFSAKFMLSE QQQPEIANVD AISVLKVLVA
DDSVLARDVL VNQLALLGIT ADAVEDGQQA LQRVLAADKS AQPYDLVILD WKMPQMDGIT
TSLHIRDQVQ NQPSHFLLVS AFHKDEAKAQ SCEAGIAQFI EKPLSRATLF NALNSLVSNT
SVESVSQKME LVSIPDLSQY KILLVEDNEI NQQVAQGFLA DTLVAVEIAE NGEVALEKVH
SQHFDLLLMD IQMPVMNGVT AAREIRSSFD AQQLPIIAMT AHAFESDAQS SFDAGMNAHI
TKPIEPEILY STLSKFLKTE KMINTSVDMN AFKATAAEMS ALTRLSEIKQ LDIGKSVERL
QGKVSLYLSL VEDFCYKHRS TSKLINQLYE KKEWKKLFLI IHSLKSTALY IGAKALAKFA
LQLEEKIEQQ HQSLLRPVNL LTGQLDDLLG QLERLYHIET QSPVDKAIDI SQSMQLIKTL
RQLLSNADPE AENISKQLYT LSSGSEFSEA IETIHLLICD FEFESALAKI DILAHAIREI
ENGN
//
