ID A0A372F620_9BACT Unreviewed; 1383 AA.
AC A0A372F620;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=D0T08_16905 {ECO:0000313|EMBL:RFS15207.1};
OS Emticicia sp. C21.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Emticicia.
OX NCBI_TaxID=2302915 {ECO:0000313|EMBL:RFS15207.1, ECO:0000313|Proteomes:UP000263688};
RN [1] {ECO:0000313|Proteomes:UP000263688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C21 {ECO:0000313|Proteomes:UP000263688};
RA Seo T., Choi J.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RFS15207.1, ECO:0000313|Proteomes:UP000263688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C21 {ECO:0000313|EMBL:RFS15207.1,
RC ECO:0000313|Proteomes:UP000263688};
RA Lis Q.M.;
RT "Emticicia ginsengisoli sp. nov.,.";
RL Submitted (SEP-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 -!- 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:RFS15207.1}.
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DR EMBL; QVMT01000007; RFS15207.1; -; Genomic_DNA.
DR OrthoDB; 9809670at2; -.
DR Proteomes; UP000263688; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00063; FN3; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003961; FN3_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; IPR013783; Ig-like_fold.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
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; PF07494; Reg_prop; 10.
DR Pfam; PF00072; Response_reg; 2.
DR Pfam; PF07495; Y_Y_Y; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; SSF63829; Calcium-dependent phosphotriesterase; 3.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:RFS15207.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:RFS15207.1}.
FT DOMAIN 867..1089
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1108..1221
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1252..1367
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1158
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1301
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1383 AA; 155254 MW; 0ABAC8E398263EBE CRC64;
MSYKVLLFSY FLLFSSAIGQ VVKPSFRHIS TNEGLSQGHV TAILKDKQGF MWFSTYEGLN
KFDGYRFFIY KHSSEDSLSL HNNIVNDILE DDAGNIWVGT ATGLDRFNRE KDNFSHFFAS
NKTVVIHEIF QDSKKRIWLG TTEGLYLINS ANGSFKVFRH EYNNKNSLSA GAVDTIEEDK
DGSLWVGTRS GLNKFNPETQ TFVHYVSDPK NPNSIGANWI KALFRDSQNN IWIGTQRGGV
SKYHVNNGTF TNFKHDPKNP NSIGYNDILS FIEDTAGNIW VGTENGGISV YGAKTKTFQT
FLNDASDISS LSNNSVYELY IDDIGNIWVG TYSGGVNFLP KFGNKFALLK EGNPVNGLKN
SSILSIAGDS EGNVWLGTDG GGLSYFDKKK NTFTTYKKQP SNPNSINSDF VTSVALIDKD
LLGVGLYLGG FDLFNKKTGQ FIHHMPDKNN PNSISSESVY AILKARDGNI WIGTLSGGLS
YYDRKTNSFT NYIHKLNDSN SIAGDFVRAL YEDDDGILWV GTDNSLDAFD KNTKKFTHFT
HKSNDKKSII NNNVQVIKEA QKGYLWIGTT DGLSLFDLKT KTFENISEKD GLPNNVINGI
LKDKKGNLWI STNKGISKYT PSTKKFRNYG ISDGLQGNEF KPASAFQTVD GEMFFGGPDG
LNTFYPDSMK DNTFIPPVHI TDFQIFNRTV GIDEKGSPLT SAISETKEIT LTHEQSVFSF
EFSALNYTLS RKNQYAYKLE GFDKDWNYIG SRRSATYTNL DPGTYTFRVK ASNNDGVWNE
EGTAITITVL PPFWETWWFR TLLVAIVIGS AIGFYRYRIG RIKAHNEKLE KQVETRTAQL
RKSTEEELKA RQDAEKANLA KSIFLATMSH EIRTPLNGII GMTSLLEETE LNEEQRNYTD
TIHTCGEGLL TVINDILDFS KIESGNMELD VKDFDLRHCI EEVLDIFAEK VAKLNIDLLY
QIDWDVPMQI IGDNLRLRQV LLNLIGNAIK FTHKGEIFIR VFLVNTGPNG QFELGFQVKD
TGIGIPADKI DKLFKAFSQV DSSTTRKYGG TGLGLVISEK LIKLMGGDIS VRSEVDKGTI
FTFTIKTEIS SVKISTLPFN LEVLENKRVL VVDDNLTNLS IFKGQLEQWK MIPTLSSSPK
EALDLVKDNN SFDIIINDMQ MPEMDGVELA LAIKKIAPKI PIMLLSSISD TFYKEHPDLF
CSVLTKPAKQ HILCRNIHNQ LLSKEQPVVV EKIKGMAAQK LSVEFAAQYP MHILVAEDYI
MNQKLALRVL SKLGYEADLA ENGMEVLEAI KHKEYDVILM DVQMPELDGL QATELIRAQM
INQPVIIAMT ANALQESRDE CLRAGMDDYI SKPINLEFLV AALEKWGTLI KKKSQEPLES
EIV
//