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Entry: A0A1I2ZTU4_9PROT
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ID   A0A1I2ZTU4_9PROT        Unreviewed;       442 AA.
AC   A0A1I2ZTU4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Phosphate regulon sensor protein PhoR {ECO:0000256|ARBA:ARBA00019665};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN05216299_11125 {ECO:0000313|EMBL:SFH40929.1};
OS   Nitrosospira sp. Nsp14.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=1855333 {ECO:0000313|EMBL:SFH40929.1, ECO:0000313|Proteomes:UP000198772};
RN   [1] {ECO:0000313|EMBL:SFH40929.1, ECO:0000313|Proteomes:UP000198772}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nsp14 {ECO:0000313|EMBL:SFH40929.1,
RC   ECO:0000313|Proteomes:UP000198772};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FOPV01000011; SFH40929.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2ZTU4; -.
DR   STRING; 1855333.SAMN05216299_11125; -.
DR   OrthoDB; 9813151at2; -.
DR   Proteomes; UP000198772; Unassembled WGS sequence.
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; IPR035965; PAS-like_dom_sf.
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   SMART; SM00091; PAS; 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; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:SFH40929.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphate transport {ECO:0000256|ARBA:ARBA00022592};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198772};
KW   Transferase {ECO:0000313|EMBL:SFH40929.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022592}.
FT   TRANSMEM        12..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          210..426
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   442 AA;  49385 MW;  4EC5D5FB1A8016A2 CRC64;
     MAGFWEHVAN VVLISVVTGM LLATLGTTVT LAIYVAALLV LLARDRRYLT ILDQWLRTEG
     SILPNASGKW GDVFARQMRL VREQSRSYQH ISSALERLQR ATSAMPEGVV ILDEMDHIEW
     CNPIAEKHLG ISSSTDTGQH ITHLVRHTQF AEYLAAQNYA EPVVVKQPRH QGLILSLQFV
     PYGDKQKLLL SRDVTQLERV QTMRQDFVAN VSHELRTPLT VIGGFLETLE DQGQSDPETF
     KWALGLMTDQ TKRMQNLVQD LLTLSRLEDT QNLIRGERVD VPAMLRKLYD EARSLSSGRH
     RISLSLDTGT QLLGSTDELR SAFTNLISNA IRYTPENGNI NLNWTIRDGQ AVFSVQDNGI
     GVEPEHISRL TERFYRVDRG RSRETGGTGL GLAIVKHVLS CHQAKLEIAS EPGKGSCFSA
     LFPAIRLVTP EGDHACTILT NL
//
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