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Database: UniProt
Entry: A0A1B2M3K2_9GAMM
LinkDB: A0A1B2M3K2_9GAMM
Original site: A0A1B2M3K2_9GAMM 
ID   A0A1B2M3K2_9GAMM        Unreviewed;       452 AA.
AC   A0A1B2M3K2;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Phosphate regulon sensor protein PhoR {ECO:0000256|ARBA:ARBA00019665};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BFG52_16415 {ECO:0000313|EMBL:AOA59776.1};
OS   Acinetobacter larvae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1789224 {ECO:0000313|EMBL:AOA59776.1, ECO:0000313|Proteomes:UP000093391};
RN   [1] {ECO:0000313|EMBL:AOA59776.1, ECO:0000313|Proteomes:UP000093391}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRTC-1 {ECO:0000313|EMBL:AOA59776.1,
RC   ECO:0000313|Proteomes:UP000093391};
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Member of the two-component regulatory system PhoR/PhoB
CC       involved in the phosphate regulon genes expression. PhoR may function
CC       as a membrane-associated protein kinase that phosphorylates PhoB in
CC       response to environmental signals. {ECO:0000256|ARBA:ARBA00025207}.
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};
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DR   EMBL; CP016895; AOA59776.1; -; Genomic_DNA.
DR   RefSeq; WP_067558847.1; NZ_CP016895.1.
DR   AlphaFoldDB; A0A1B2M3K2; -.
DR   STRING; 1789224.BFG52_16415; -.
DR   KEGG; ala:BFG52_16415; -.
DR   OrthoDB; 9813151at2; -.
DR   Proteomes; UP000093391; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
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; 3.30.450.20; PAS domain; 1.
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; IPR000014; PAS.
DR   InterPro; IPR021766; PhoR.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR014310; Sig_transdc_His_kinase_PhoR.
DR   NCBIfam; TIGR02966; phoR_proteo; 1.
DR   PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13188; PAS_8; 1.
DR   Pfam; PF11808; PhoR; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
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; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Kinase {ECO:0000313|EMBL:AOA59776.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphate transport {ECO:0000256|ARBA:ARBA00022592};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000093391};
KW   Transferase {ECO:0000313|EMBL:AOA59776.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022592}.
FT   TRANSMEM        25..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          231..447
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   452 AA;  51636 MW;  CBEBC7149D54499B CRC64;
     MYEPYPVPEL ARDHKKSRYS SLRTFAKQDL KLLAFLLIIA AFIGYGTGYF LLCAVFAFAV
     FFAFQLYSLY LVNEWISNRP YEVPPNLNGI WGALLFNFYR AQRQERVVQA EMVGLIDRAQ
     SSLVALAEAV VLTDELHQIE WANPAAEALL GIQALDRGRN LLTILRHPRF IEYFSHIDQY
     PDGIRVKLSI EDEKYVQIKL TRFGSESLLL VAYDVTRMQN LEQMRKDFVD NISHELRTPL
     TVLSGYIETF TDQEDISPRW KRAFDQMQSQ TRRMNALVND LLLLSRLENE KQIPKNQIIE
     MPSLMNQLFD DAQAYNADYG HTLNLEIDSH YDLIGSDMEI ASAFSNLITN AIKYTPKGGS
     ITIGWHDDGE QAYFSVEDTG IGINPKHLPR LTERFYRVDS ARSRQSGGTG LGLAIVKHVL
     MQHAAHLEVE SVENQGSVFK AVFPKSALYF VD
//
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