ID A0A0D8PW46_9GAMM Unreviewed; 442 AA.
AC A0A0D8PW46;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Phosphate regulon sensor protein PhoR {ECO:0000256|ARBA:ARBA00019665};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C9I88_19150 {ECO:0000313|EMBL:PSV89143.1};
OS Photobacterium iliopiscarium.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=56192 {ECO:0000313|EMBL:PSV89143.1, ECO:0000313|Proteomes:UP000241954};
RN [1] {ECO:0000313|EMBL:PSV89143.1, ECO:0000313|Proteomes:UP000241954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 13481 {ECO:0000313|EMBL:PSV89143.1,
RC ECO:0000313|Proteomes:UP000241954};
RA Butler K.;
RT "Whole genome sequencing of Histamine producing bacteria.";
RL Submitted (JAN-2018) 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};
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:PSV89143.1}.
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DR EMBL; PYLW01000035; PSV89143.1; -; Genomic_DNA.
DR RefSeq; WP_045037156.1; NZ_PYOP01000019.1.
DR AlphaFoldDB; A0A0D8PW46; -.
DR STRING; 56192.UB38_15070; -.
DR Proteomes; UP000241954; 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 GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 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; IPR013767; PAS_fold.
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; PF00989; PAS; 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:PSV89143.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphate transport {ECO:0000256|ARBA:ARBA00022592};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:PSV89143.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022592}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 211..428
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 442 AA; 50904 MW; BF75BA1E3481ACF0 CRC64;
MERLTWKKLV GELILFYLPW LILGVIFGYL PWFLLIASWI QLGWHFHNQL KMSNWLWKDR
SLTPPSGSGS WEPLFNGIYR LQQRNRRRRK ELTTLIRRFR NGAESLPDAV VVFRSEGNIV
WCNKLAQQLL GLRWPDDSGQ PISNLLRSPD FVRYLSRQAF DTPLEITSPM NYDRTLELRI
MRYTEGEYLM AVRDVSQLKQ LEGMRRNFFA NVSHELRTPM TVLQGYLEMA QDPEMLMGPM
WDRAHGVMTE QLARMNALVE QLLTLSKIEA APTIELEEMV DVPAMLDILE KEAMSLSSNK
DQSFTFDVDN SLKVFGDNDQ LRSAISNLVY NAVKHTPNDA AIHVRWYRSP TGPRLEVTDS
GEGIEAQHIH RLTERFYRVD KARSRETGGS GLGLAIVKHA LSHHDAHLEI ESEIDKGSTF
SFTLPSRLVV DTTLPHTATN DH
//
