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Database: UniProt
Entry: A9IF18_BORPD
LinkDB: A9IF18_BORPD
Original site: A9IF18_BORPD 
ID   A9IF18_BORPD            Unreviewed;       460 AA.
AC   A9IF18;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Sensor protein {ECO:0000256|RuleBase:RU364088};
DE            EC=2.7.13.3 {ECO:0000256|RuleBase:RU364088};
GN   Name=copS {ECO:0000313|EMBL:CAP44944.1};
GN   OrderedLocusNames=Bpet4593 {ECO:0000313|EMBL:CAP44944.1};
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP44944.1, ECO:0000313|Proteomes:UP000001225};
RN   [1] {ECO:0000313|EMBL:CAP44944.1, ECO:0000313|Proteomes:UP000001225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC   {ECO:0000313|Proteomes:UP000001225};
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA   Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA   Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA   Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA   Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA   Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA   Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the metabolic
RT   versatility of environmental bacteria and virulence traits of pathogenic
RT   Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
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; AM902716; CAP44944.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9IF18; -.
DR   STRING; 94624.Bpet4593; -.
DR   KEGG; bpt:Bpet4593; -.
DR   eggNOG; COG2205; Bacteria.
DR   eggNOG; COG3850; Bacteria.
DR   Proteomes; UP000001225; 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; cd06225; HAMP; 1.
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; SENSOR HISTIDINE KINASE YKOH; 1.
DR   PANTHER; PTHR45436:SF9; SENSOR PROTEIN; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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   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        153..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364088"
FT   DOMAIN          181..234
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          242..455
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   460 AA;  50749 MW;  D55AFAFD83E782F6 CRC64;
     MRLLPTNSIQ VRLTLLLGLI ALVVSTVAGC TLFLALKREV QRQEMTEVSG KLELIDHMVD
     MQTEPSQYDG LRQTLDGILV GHTNLRVWII RPNGEVFYGA EAPQITRVFS DGEVSLQTQD
     GLHMRGMQAA LDGKLFPQGQ LLVAVNVRPS AEFLYAFATA LVLICIIWIG VTVILSAWAV
     RRSLAPIRRL SARAAQIGPD NLKVRLPEGG IDRELREFTH TFNKMLARVQ AAYQQMEGFN
     ADVAHELRTP LATLINGTEV TLSSERSIEE LRDVMASNLE ELHGLKALIN DMLFLARADG
     GETARDLRPV MVRDEIDQVV EYYEAALEEA GVRLVVDGNV QVHANSRLLR RAIANLVSNA
     IKATPNGQTI LARCAQDDQF VEISLRNPGT PIHRDALPRI FDRFFRADDA RSGRADGHGL
     GLAIVSAIAR MHGGAAFAKS DNHGSEVGFT IQRDQDITKK
//
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