ID B9XKB2_PEDPL Unreviewed; 444 AA.
AC B9XKB2;
DT 14-APR-2009, integrated into UniProtKB/TrEMBL.
DT 14-APR-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Cflav_PD2571 {ECO:0000313|EMBL:EEF59750.1};
OS Pedosphaera parvula (strain Ellin514).
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Limisphaerales; Pedosphaera.
OX NCBI_TaxID=320771 {ECO:0000313|EMBL:EEF59750.1, ECO:0000313|Proteomes:UP000003688};
RN [1] {ECO:0000313|EMBL:EEF59750.1, ECO:0000313|Proteomes:UP000003688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin514 {ECO:0000313|EMBL:EEF59750.1,
RC ECO:0000313|Proteomes:UP000003688};
RX PubMed=21460084; DOI=10.1128/JB.00299-11;
RA Kant R., van Passel M.W., Sangwan P., Palva A., Lucas S., Copeland A.,
RA Lapidus A., Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Larimer F.W., Land M.L., Hauser L., Brettin T.S.,
RA Detter J.C., Han S., de Vos W.M., Janssen P.H., Smidt H.;
RT "Genome sequence of 'Pedosphaera parvula' Ellin514, an aerobic
RT Verrucomicrobial isolate from pasture soil.";
RL J. Bacteriol. 193:2900-2901(2011).
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:EEF59750.1}.
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DR EMBL; ABOX02000024; EEF59750.1; -; Genomic_DNA.
DR AlphaFoldDB; B9XKB2; -.
DR STRING; 320771.Cflav_PD2571; -.
DR Proteomes; UP000003688; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_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; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43711:SF31; SENSOR HISTIDINE KINASE GRAS; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000003688}.
FT DOMAIN 77..197
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 224..434
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 444 AA; 48873 MW; 3B0AA5FB14E2997C CRC64;
MLRIACGNYS GGGLVGGSGR KAVRGWSRGA LQSASRGSAA IVKEREKGGW LGVSCLLYGR
GFWLKLGGMM TLESCPIFSQ LKPGELKVLE QAAQVRGFKA NEDIFREGDT GDGVYVVRRG
LVQITGLITL NDRHAFSKVG PGEMFGEMAV LENKPRSASA TALEETEVYF IPREAMLALV
ENSPLLSMGL LREISNRLRE FNRQYVSEVL QRERLALVGR FARTIVHDLK NPLNIIGLSA
EMAGMEKATP EGRHLAKQRI SKQVERISEL VNEILEFTQG SHVSFVLAQT PYDVFVQILL
EEIRPEIEIK SVTIELENAP PAIRLLLNPK RLRRVFYNLI HNATDAMPDG GRITLRFRVS
EEEVITEIED TGPGIATEIA DRLFDAFATF GKAHGTGLGL SISKKIVEDH RGRISARNEP
GRGAVFSFAL PVPAGEHEEA VIGR
//
