ID A0A261UGK9_9BORD Unreviewed; 476 AA.
AC A0A261UGK9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Sensor protein {ECO:0000256|RuleBase:RU364088};
DE EC=2.7.13.3 {ECO:0000256|RuleBase:RU364088};
GN ORFNames=CAL28_14780 {ECO:0000313|EMBL:OZI60657.1};
OS Bordetella genomosp. 11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1416808 {ECO:0000313|EMBL:OZI60657.1, ECO:0000313|Proteomes:UP000215767};
RN [1] {ECO:0000313|EMBL:OZI60657.1, ECO:0000313|Proteomes:UP000215767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU8856 {ECO:0000313|EMBL:OZI60657.1,
RC ECO:0000313|Proteomes:UP000215767};
RA Spilker T., LiPuma J.;
RT "Complete and WGS of Bordetella genogroups.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Member of a two-component regulatory system.
CC {ECO:0000256|RuleBase:RU364088}.
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 ECO:0000256|RuleBase:RU364088};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|RuleBase:RU364088}.
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:OZI60657.1}.
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DR EMBL; NEVS01000004; OZI60657.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261UGK9; -.
DR OrthoDB; 9786919at2; -.
DR Proteomes; UP000215767; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR006290; CztS_silS_copS.
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 NCBIfam; TIGR01386; cztS_silS_copS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR PANTHER; PTHR45436:SF9; SENSOR PROTEIN; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|RuleBase:RU364088};
KW Cell inner membrane {ECO:0000256|RuleBase:RU364088};
KW Cell membrane {ECO:0000256|RuleBase:RU364088};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU364088};
KW Membrane {ECO:0000256|RuleBase:RU364088};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU364088};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364088};
KW Transmembrane {ECO:0000256|RuleBase:RU364088};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364088};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012,
KW ECO:0000256|RuleBase:RU364088}.
FT TRANSMEM 153..180
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364088"
FT DOMAIN 181..234
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 242..459
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 456..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 476 AA; 51814 MW; C2D27CD4F4776EDC CRC64;
MKPPRVTSIS GRLTLFLAAI ALCVSSIAGY TLFLALKYEV QRREMAEVAG KLELIDHLIG
MQSTPEELGT LKGTLDNILV GHPNLKVWLM DTDGRVLYGD VPPRSIQPSR GREVLLETAT
GARMRALQVP VRSQAAPDAL LTVAIDTQPS ADFLYGFASV LAAICVFWVG ASALLGAWAV
RRSLAPVHRL SHQAARVQPE QLDLRLPVQG IDRELRELSI AFNSTLDRLQ AAYRQLEGFN
ADVAHELRTP LATLINGTEI VLASDRSNDE LREVLESNLE ELVGLKALIN DMLFLARADG
GELARDLREV QIAAEIRHVA DYHEAALQEA GLTLRQAGDA RVRANPRLLR RALSNLIANA
IKASPAHTAL EITCMESLTD VEIRVVNAGE AIPPNALPRI FDRFYRVDDA RTGRSEGHGL
GLAIVRAIAR MHGGRVFAHS EAGRTIVGFT LSRLRPSTPA RTGDPDSAAA LAQPRI
//
