ID A0A1G7SFR8_9FLAO Unreviewed; 1202 AA.
AC A0A1G7SFR8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05421825_2960 {ECO:0000313|EMBL:SDG21754.1};
OS Epilithonimonas hungarica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Epilithonimonas.
OX NCBI_TaxID=454006 {ECO:0000313|EMBL:SDG21754.1, ECO:0000313|Proteomes:UP000199203};
RN [1] {ECO:0000313|Proteomes:UP000199203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19684 {ECO:0000313|Proteomes:UP000199203};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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};
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DR EMBL; FNBH01000003; SDG21754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7SFR8; -.
DR STRING; 454006.SAMN05421825_2960; -.
DR OrthoDB; 9811889at2; -.
DR Proteomes; UP000199203; Unassembled WGS sequence.
DR GO; GO:0016020; C: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; cd14686; bZIP; 1.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd19410; HK9-like_sensor; 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; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR007891; CHASE3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
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; PF05227; CHASE3; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SDG21754.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 180..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 220..272
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 532..754
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 814..927
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 936..1052
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1082..1199
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 432..508
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 863
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 985
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1132
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1202 AA; 135899 MW; 0292EF5DAB9BD75A CRC64;
MPKKIIRNLQ FGVGLSLLIL LASSLASYLS IQNQMNNREK SSQSRRSITA VKDVLIALLD
AETGNRGYQL TGKESFLEPY NRSVSEYAKA IDRAKEIEIT DKLQLKRVED LQQNANNSME
NLRQFVINRR NGLPMTQEQI TSSKVYMDRC RQIVADFVKY EESQLVIKNK ALNNSSSTTV
LFIIFSAITA VVVTIFFYTR LRNDLIRRDR LEKELMAKDL EISKRVSIIK QVTSKVASGD
YSVRLSDRGE DELADIVESL NYMTQSLKTS FEQINENEWR QKGLVLLNES LVGNKTVKEV
TDNALDHFVS YADCVNGAIY LYEDERLRLY KAFGLEEYMK KSFLPGEGMV GQTFVKEKTN
VFNDLGDKDF VASFASSKIR IQGIILVPIM LGRQIFGILE LGATHNFDAV KIDYFNEGAR
NIATALSAAR SREKEQRLLE ETQAQSEELQ VQHAELENLN TELEAQTQKL QASEEELRVQ
QEELLQTNTE LEERSKALEE KNHLIAERNI EIQKKAEELA LSTQYKSEFL ANMSHELRTP
LNSILLLSRL MAENPEENLN EDQIESAKVI QSSGTSLLTL IDEILDLAKI ESGKMNLVNE
PILLDDVTRD LKNLFMPIVK EKGVQFNIYL DDSITRTLST DRLRLDQVLR NLLSNAFKFT
KEGSVDLNIY DCPKNSEFIV FSVKDTGMGI PEEKQKLIFE AFQQADGSTQ RKFGGTGLGL
SISREIAKLL GGKITLESES GKGSEFSLII PKQPSDSSGI ISNEQSLIDV ISQDVEEIKT
IIETDDQNIA SIAHLEIPEE IEDDRNNISK GDKVILIIED DTHFAKALLK YAHVNDYKAV
IIVRGDYALP AALEYKPVAI LLDIQLPVKD GWQVMNDLKT NSQTRPVPVH MMSSLQAKRE
SLMRGAIDFI DKPVAIEEMN NVFKKIEDAL KRSPQKVLIV EENAQHAKAL SYFLGNYNIS
LSVENNVEDS VKAFQKDNVD CVIVDVGSAR GSSYQIVERI KSYEGLENLP VIIFTERNLT
QSEELKIKQY ADSIVVKTAH SYQRILDEIS LFLHLVEENN QSGESGRVKN LGTLTETLSG
KKILITDDDV RNIFSLSKAL EKYKVEVVLA MDGKQALDKI EENPDIDVIL MDMMMPEMDG
YDTIREIRKM PDFKDLPIIA VTAKSMIGDR DKCIQAGASD YITKPVDIDQ LLSLLRVWLY
ES
//
