ID V2UDL0_9GAMM Unreviewed; 881 AA.
AC V2UDL0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=P255_00724 {ECO:0000313|EMBL:ESK52568.1};
OS Acinetobacter brisouii CIP 110357.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1341683 {ECO:0000313|EMBL:ESK52568.1, ECO:0000313|Proteomes:UP000018418};
RN [1] {ECO:0000313|EMBL:ESK52568.1, ECO:0000313|Proteomes:UP000018418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 110357 {ECO:0000313|EMBL:ESK52568.1,
RC ECO:0000313|Proteomes:UP000018418};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Grillot-Courvalin C.,
RA Clermont D., Rocha E., Yoon E.-J., Nemec A., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter brisouii CIP 110357.";
RL Submitted (OCT-2013) 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:ESK52568.1}.
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DR EMBL; AYEU01000003; ESK52568.1; -; Genomic_DNA.
DR RefSeq; WP_004903662.1; NZ_KI530762.1.
DR AlphaFoldDB; V2UDL0; -.
DR PATRIC; fig|1341683.3.peg.717; -.
DR HOGENOM; CLU_000445_113_2_6; -.
DR OrthoDB; 9806130at2; -.
DR Proteomes; UP000018418; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; cd01987; USP_OKCHK; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR029016; GAF-like_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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF02702; KdpD; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000018418};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 405..438
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 445..463
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 663..880
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 881 AA; 99276 MW; D994C724DC769125 CRC64;
MQIDRNNKAD AWLAHSQREQ SGRLTIFLGA APGVGKTYAM LTRAHELMQQ GQHVVVGVVE
THGRSDTERL IQGLHVIPRK SLEYQGRMLE EMDLDQILKL KPQIVLVDEL AHRNVPNSRH
EYRWQDVNEL LDAGIDVYST LNIQHLESLN DVVYQITGIR VTETVPDALL KRLKDIRLVD
LPVPELLERM NHGKIYFADV APHALQGFFK AANLTALRDL AIQTVAGQVD IDYREKFVAQ
GQIIPIQNHV LLAIDGSEFS EDLVRRAHRI AERRNATWSV ISIQKSKAET TQIFTVTKAF
NLARKLGADT YLLYSNHIAS TILQAAYDYG ASNILLGKSP QKSLWQRLFS DHIADQLLEK
QHPFEITFVQ PLKAQNNQTS PNDAAHSSWR EQGLAFTQRE VFESIIIVLL GLIVAAISDH
FIGYSDLALI FIVTVLLVAI RARMLITIIS VFICFLLYNY FFIEPRFTFM ISAERGVITI
ITFIVSALLV GRLANQLRAQ VLSLRAANSV SLQLQELERK LSACVDIEQV LNVAKQHLET
SLNATVWLKV ENQSLGDPSV LNEKDQIAAD WTQKNAKPCG RFTNTLTNSD WWFIPLNLVK
EYGVIAIRFN QNAQTISFEL QRLTELMIED IAQTVARVQL SLQLENSRVV AETEKLRSAL
LSSVSHDLRS PLAAMIGSAD TLKYYGEQMS ESDRHELLDT IHIEGERLDR YIQNLLDMTR
LGHQGLTLAR DWIGVDELIG SATQRLKRYQ PNVKIDVTLA DDLPQLYVHP ALIEQAIFNV
LENAAKFSPD DMPIKISIQQ EDDFLQINIE DQGVGIPEDE REQIFDMFYT MQRGDRGKTG
TGLGLAIVKA IIGAHMGSIE ALAGTHGQGT LIKIRLPLHQ D
//
