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Database: UniProt
Entry: M9WV35_SERS3
LinkDB: M9WV35_SERS3
Original site: M9WV35_SERS3 
ID   M9WV35_SERS3            Unreviewed;       486 AA.
AC   M9WV35;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=gvrB {ECO:0000313|EMBL:AGJ98304.1};
GN   ORFNames=CWC46_01195 {ECO:0000313|EMBL:AUG98558.1}, Ser39006_001195
GN   {ECO:0000313|EMBL:AUH02873.1};
OS   Serratia sp. (strain ATCC 39006).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=104623 {ECO:0000313|EMBL:AGJ98304.1};
RN   [1] {ECO:0000313|EMBL:AGJ98304.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21873216; DOI=10.1073/pnas.1109169108;
RA   Ramsay J.P., Williamson N.R., Spring D.R., Salmond G.P.;
RT   "A quorum-sensing molecule acts as a morphogen controlling gas vesicle
RT   organelle biogenesis and adaptive flotation in an enterobacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:14932-14937(2011).
RN   [2] {ECO:0000313|EMBL:AUH02873.1, ECO:0000313|Proteomes:UP000017700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39006 {ECO:0000313|EMBL:AUH02873.1}, and ATCC 39006 / SC
RC   11482 {ECO:0000313|Proteomes:UP000017700};
RX   PubMed=24336377; DOI=10.1128/genomeA.01039-13;
RA   Fineran P.C., Iglesias Cans M.C., Ramsay J.P., Wilf N.M., Cossyleon D.,
RA   McNeil M.B., Williamson N.R., Monson R.E., Becher S.A., Stanton J.A.,
RA   Brugger K., Brown S.D., Salmond G.P.;
RT   "Draft genome sequence of Serratia sp. strain ATCC 39006, a model bacterium
RT   for analysis of the biosynthesis and regulation of prodigiosin, a
RT   carbapenem, and gas vesicles.";
RL   Genome Announc. 1:E01039-E01039(2013).
RN   [3] {ECO:0000313|EMBL:AGJ98304.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Ramsay J.P., Williamson N.R., Spring D.R., Salmond G.P.C.;
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AUH02873.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 39006 {ECO:0000313|EMBL:AUH02873.1};
RA   Wang G., Yang Y., Su Y.;
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:AUG98558.1, ECO:0000313|Proteomes:UP000233778}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39006 {ECO:0000313|EMBL:AUG98558.1,
RC   ECO:0000313|Proteomes:UP000233778};
RA   Hampton H.G., Jackson S.A., Jauregui R., Poulter G.T.M., Salmond G.P.C.,
RA   Fineran P.C.;
RT   "Complete genome sequence of Serratia sp. ATCC 39006 LacA.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:AUH02873.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 39006 {ECO:0000313|EMBL:AUH02873.1};
RA   Hampton H.G., Jackson S.A., Jauregui R., Poulter G.T.M., Salmond G.P.C.,
RA   Fineran P.C.;
RT   "Complete genome sequence of Serratia sp. ATCC 39006.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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; KC601845; AGJ98304.1; -; Genomic_DNA.
DR   EMBL; CP025085; AUG98558.1; -; Genomic_DNA.
DR   EMBL; CP025084; AUH02873.1; -; Genomic_DNA.
DR   RefSeq; WP_021013990.1; NZ_CP025085.1.
DR   AlphaFoldDB; M9WV35; -.
DR   STRING; 104623.Ser39006_00715; -.
DR   KEGG; sera:Ser39006_001195; -.
DR   KEGG; serq:CWC46_01195; -.
DR   eggNOG; COG4191; Bacteria.
DR   OrthoDB; 1931120at2; -.
DR   Proteomes; UP000017700; Chromosome.
DR   Proteomes; UP000233778; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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; 2.
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; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 2.
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); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AUG98558.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017700};
KW   Transferase {ECO:0000313|EMBL:AUG98558.1}.
FT   DOMAIN          138..208
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          211..264
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          277..486
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   486 AA;  53854 MW;  867CE9555AA904E0 CRC64;
     MSDNPFEQQS ENHFELLYNM LLDAIPSSVL MVDEKLHVVS VNQNFLIKGH RGNPDTIGRP
     LSDVFPSVIL ENTGLEAHIR DVFRSGLPVN GQKMTYRAPG VPIRIYYYSI LPIPINQIML
     FMEDVTEQVR LSEEVHRVER HLASVVENAS DIVLSTDIEG CILTWNSAAE KLSGLPTHEV
     YGRYFFEFCD TNQKEAVRLI FMRMKNSNES HTTEFHLLTP NNGGSILISW VFSPMKDDYG
     QTVGTVVVGR DLAERRKLEL QLRQSQKLTA LGVMAGGIAH EIRNPLAVCS SAAQFLLEDE
     ITAEFHKECS RKIQTNIQKA SAIIENLLRF ARSSLDTEMV EVNLITVLKE TIDLIANQAK
     VQKIQILLPL QKGNILVSGV SGLLQQVFMN IFLNAINAMP EGGVLSIAVE TFEDRVIVRI
     SDTGVGIPAG ELDKIFDPFH TSSPVGQGTG LGLSICYSII QQHLGSIQAE SCLGEGSTII
     VTLPIL
//
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