ID G0AHI3_COLFT Unreviewed; 470 AA.
AC G0AHI3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Sensor protein {ECO:0000256|RuleBase:RU364088};
DE EC=2.7.13.3 {ECO:0000256|RuleBase:RU364088};
GN OrderedLocusNames=CFU_0184 {ECO:0000313|EMBL:AEK60022.1};
OS Collimonas fungivorans (strain Ter331).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Collimonas.
OX NCBI_TaxID=1005048 {ECO:0000313|EMBL:AEK60022.1, ECO:0000313|Proteomes:UP000008392};
RN [1] {ECO:0000313|EMBL:AEK60022.1, ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|EMBL:AEK60022.1,
RC ECO:0000313|Proteomes:UP000008392};
RX PubMed=15305924; DOI=10.1111/j.1462-2920.2004.00673.x;
RA Leveau J.H., Gerards S., de Boer W., van Veen J.A.;
RT "Phylogeny-function analysis of (meta)genomic libraries: screening for
RT expression of ribosomal RNA genes by large-insert library fluorescent in
RT situ hybridization (LIL-FISH).";
RL Environ. Microbiol. 6:990-998(2004).
RN [2] {ECO:0000313|EMBL:AEK60022.1, ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|EMBL:AEK60022.1,
RC ECO:0000313|Proteomes:UP000008392};
RX PubMed=16457898; DOI=10.1016/j.mimet.2005.12.010;
RA Leveau J.H., Gerards S., Fritsche K., Zondag G., van Veen J.A.;
RT "Genomic flank-sequencing of plasposon insertion sites for rapid
RT identification of functional genes.";
RL J. Microbiol. Methods 66:276-285(2006).
RN [3] {ECO:0000313|EMBL:AEK60022.1, ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|EMBL:AEK60022.1,
RC ECO:0000313|Proteomes:UP000008392};
RX PubMed=18671744; DOI=10.1111/j.1574-6941.2008.00547.x;
RA Fritsche K., de Boer W., Gerards S., van den Berg M., van Veen J.A.,
RA Leveau J.H.;
RT "Identification and characterization of genes underlying chitinolysis in
RT Collimonas fungivorans Ter331.";
RL FEMS Microbiol. Ecol. 66:123-135(2008).
RN [4] {ECO:0000313|EMBL:AEK60022.1, ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|EMBL:AEK60022.1,
RC ECO:0000313|Proteomes:UP000008392};
RX PubMed=19638176; DOI=10.1111/j.1462-2920.2009.02010.x;
RA Leveau J.H., Uroz S., de Boer W.;
RT "The bacterial genus Collimonas: mycophagy, weathering and other adaptive
RT solutions to life in oligotrophic soil environments.";
RL Environ. Microbiol. 12:281-292(2010).
RN [5] {ECO:0000313|EMBL:AEK60022.1, ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|EMBL:AEK60022.1,
RC ECO:0000313|Proteomes:UP000008392};
RX PubMed=21614084; DOI=10.1038/ismej.2011.29;
RA Mela F., Fritsche K., de Boer W., van Veen J.A., de Graaff L.H.,
RA van den Berg M., Leveau J.H.;
RT "Dual transcriptional profiling of a bacterial/fungal confrontation:
RT Collimonas fungivorans versus Aspergillus niger.";
RL ISME J. 5:1494-1504(2011).
RN [6] {ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|Proteomes:UP000008392};
RA Leveau J.H.;
RT "Complete sequence of Collimonas fungivorans Ter331.";
RL Submitted (MAY-2011) 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}.
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DR EMBL; CP002745; AEK60022.1; -; Genomic_DNA.
DR RefSeq; WP_014004177.1; NC_015856.1.
DR AlphaFoldDB; G0AHI3; -.
DR STRING; 1005048.CFU_0184; -.
DR KEGG; cfu:CFU_0184; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_89_6_4; -.
DR Proteomes; UP000008392; Chromosome.
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; 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:SF3; SENSOR HISTIDINE KINASE HPRS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 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 Reference proteome {ECO:0000313|Proteomes:UP000008392};
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 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364088"
FT TRANSMEM 168..191
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364088"
FT DOMAIN 192..245
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 253..467
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 470 AA; 51731 MW; 9AB0CF35BDD6A7D7 CRC64;
MNAWRRQSLT ARVTFLFALI ACAIVATLGM YLYSSTRQAL ETRADYSLIG KVEHFRHLLH
DLYNVKQMED SPTLFETMLG SEQDVLIFAY PGQAPFVRVN PDHMTPPPMT PQSLDQPLTL
AQLHAGVRAD GVRVRWVSAL ADVGGDGTQV VITGAHVMTQ ESHILARYYW QVIGAAAVAV
LLAALLGFLV LKRGFLPLTA MACRAAEVSP TNIAIRLREE DAPHELRRLA ASFNAMLDRL
ADGYEHLSQF SADLAHEIRT PIGALMGQTQ VTLGQVRNAA EYQQVLESNL EELQRLSRIV
ENILFLAHAD HAGLAVEKTP LVLADELHKI ADYFEGVAEE RGIRLEVDAS GKVQASPVMW
RRAVSNLVVN AVRYAAPGST VRLSGRPQAQ GIDVAVENQG DPIPPEQLER LFDRFYRGDQ
SRSEYTESNG LGLAIVRAIM LVHGGSAEVA CSREGLIRFS LYFPEGAETV
//
