ID A0A2U2B3K0_9BACT Unreviewed; 1271 AA.
AC A0A2U2B3K0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DDZ16_19750 {ECO:0000313|EMBL:PWD97624.1};
OS Marinilabilia rubra.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC Marinilabilia.
OX NCBI_TaxID=2162893 {ECO:0000313|EMBL:PWD97624.1, ECO:0000313|Proteomes:UP000244956};
RN [1] {ECO:0000313|EMBL:PWD97624.1, ECO:0000313|Proteomes:UP000244956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WTE16 {ECO:0000313|EMBL:PWD97624.1,
RC ECO:0000313|Proteomes:UP000244956};
RA Zhang R.;
RT "Marinilabilia rubrum sp. nov., isolated from saltern sediment.";
RL Submitted (MAY-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:PWD97624.1}.
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DR EMBL; QEWP01000030; PWD97624.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2B3K0; -.
DR OrthoDB; 717811at2; -.
DR Proteomes; UP000244956; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00146; PKD; 1.
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; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
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; IPR013783; Ig-like_fold.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
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; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF07494; Reg_prop; 3.
DR Pfam; PF00072; Response_reg; 1.
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; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000244956};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 803..822
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 911..1129
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1153..1268
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 842..897
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1203
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1271 AA; 147065 MW; 97DD9B2D167DC1EC CRC64;
MLLTKKKAAM YRHLNILFLL LIFCSELILA NEKIKLKPLE SELFQSLVRD IHRDHEGYLW
IANNGVGLMK YNSHFITRYL HNKSDTTSMS DDGVMVIEQD SMKNLWFGTI NGLNRYCTYQ
DNFERYFSIP GDTTSLSSNF VNEMYLDTRG TLWVLTAHGL CQYLPEKNHF KRFYIPDSPS
ANNFTGMDQD SKGNYWVVTT SNGIYKFNPD SNLFIHYPDN KTISERLFSK KILIDTKDRF
WIANWGAGLA SFNPEAGDYF YYPVTDDGSG TNRNLAMNII EWGNDQLLIA VDQGGINKLD
LKTNIFTYIK ANDPAYGQML SNGVYCFHHD QEGILWVGTS RGGTFYSNPK ENIFDIYSTY
GGSMAVKDGI YNMPIHNIIT SFYEDAKGDI WVGTGGGGIA SFNQQERKFI FHTHNPQNEN
SLSSNVIRTI TGDHNGNLLV ATWDGGINKM NPQTGMFTKE PFERKLDGGY HGRNLWNIDT
DSKNRIWITN PVGQIDLYDE NKNLLGQFFI EPNPEIYHLP LIYEDEKNRI YTNTVRGVFL
FNESGRYFEQ VIKLPEVTFI NLDDPKHIWA GTQKDGLYLC SRNGQILKQY TTEDGLSDNY
VCSIIMDSER NLWISTHNGL SYLKTKAEQF TNYTEKDALA GNHFYIQSSL KTSNGKIFFG
GADGFISFFP KDIPENKTRP EIYLTDFYVN NKKMDFKEEK SPISKPVKYI KNVNLKYNQR
ILTFHFQSIN YTFPHKSQYK YILEGYENEW HVQNTEVTSA NYTNLDPGTY TFKVTASNSD
GLWSKKPATM EILIRPPVWK TRLFLVALTV IIIASLVLLL KWRNRKLIRE KNRLQKKVSE
RTKVIEEQAH ELSNQNRILE DQKEELEIQR DELAKHEEIL EQEVRERTRD LKIAKDKAEK
SDKLKSYFLA NMSHEIRTPM NAIVGFATLL NEEGTSPEEK SEFIKLIKDN SDNLRFLVED
ILDFSLIEAN QMKIHYNNFL LNEFINHIYS SFALRNENPN VELRKKNLLE KEDLSFISDE
FRIRQILSNL LSNAIKFTEH GFVELIIDRK ASEIVFSVTD TGPGISESEQ KIIFNQFVKL
ENDQFMAKRG IGLGLTLSQR LSKMLGAKLS VESELGKGST FSLSFPFNVT MSRRTYPPKK
PTTFLRKNWS YKNLLVIEDE ISNYHFIFEV LKGTEINITW AKDGFEALEF LHNSKKFDLV
LLDIKLPKMD GFKTFQRIRE LVPEQIIIAQ TAYARPEDEL KIRESGFDEY LAKPINPHHL
LKILSQFLDN N
//
