NODV_BRADU
ID NODV_BRADU Reviewed; 889 AA.
AC P15939;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 25-MAY-2022, entry version 167.
DE RecName: Full=Nodulation protein V;
DE EC=2.7.13.3;
GN Name=nodV; OrderedLocusNames=bll1715;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=USDA 110spc4;
RX PubMed=2320582; DOI=10.1073/pnas.87.7.2680;
RA Goettfert M., Grob P., Hennecke H.;
RT "Proposed regulatory pathway encoded by the nodV and nodW genes,
RT determinants of host specificity in Bradyrhizobium japonicum.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2680-2684(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=USDA 110spc4;
RX PubMed=11157954; DOI=10.1128/jb.183.4.1405-1412.2001;
RA Goettfert M., Roethlisberger S., Kuendig C., Beck C., Marty R.,
RA Hennecke H.;
RT "Potential symbiosis-specific genes uncovered by sequencing a 410-kb DNA
RT region of the Bradyrhizobium japonicum chromosome.";
RL J. Bacteriol. 183:1405-1412(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
CC -!- FUNCTION: Member of the two-component regulatory system NodV/NodW
CC probably involved in the regulation of the transcription of genes
CC involved in the nodulation process. NodV may function as a membrane-
CC associated protein kinase that phosphorylates NodW in response to
CC environmental signals.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
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DR EMBL; M31765; AAA26231.1; -; Genomic_DNA.
DR EMBL; AF322012; AAG60698.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC46980.1; -; Genomic_DNA.
DR PIR; A35989; A35989.
DR RefSeq; NP_768355.1; NC_004463.1.
DR RefSeq; WP_011084527.1; NZ_CP011360.1.
DR AlphaFoldDB; P15939; -.
DR SMR; P15939; -.
DR STRING; 224911.27349968; -.
DR EnsemblBacteria; BAC46980; BAC46980; BAC46980.
DR GeneID; 64067028; -.
DR KEGG; bja:bll1715; -.
DR PATRIC; fig|224911.44.peg.1178; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_39_5; -.
DR InParanoid; P15939; -.
DR OMA; VRITMAL; -.
DR PhylomeDB; P15939; -.
DR BRENDA; 2.7.13.3; 929.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; IBA:GO_Central.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 4.
DR Gene3D; 1.20.120.620; -; 1.
DR Gene3D; 3.30.565.10; -; 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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55785; SSF55785; 4.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Nodulation; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..889
FT /note="Nodulation protein V"
FT /id="PRO_0000074819"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 132..202
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 206..257
FT /note="PAC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 332..383
FT /note="PAC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 384..456
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 460..512
FT /note="PAC 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN ?..593
FT /note="PAS 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 594..646
FT /note="PAC 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 669..885
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 889 AA; 99158 MW; 37129701CF9DCDE7 CRC64;
MYRISSFKRS APQLTLGSIA LAAVTLTCVY FQAHFAAAAF AYLLVVLLFS LMGSFIASSA
LCIVAIAALA YYFAPPAFSL RIDDPRDVPV VVAFLIVSVV GTYLIGKLRQ EREAARVAAA
KLQRSASDLE DREKRWRAIF EHNPAMYFMV DEAGIVLNVN TLGATQLGFA CAELLGQSVL
DVFLEEDRAF VRKCIQTCLE DVGQSRTWDV RKVRKDGSVL WVRENAKAML WAGDRPVILM
ACEDITERKQ TELALQRSEA HLAHAQELSH TGSFSWNAST GEAFWSKETF RIFQIDLQTT
PAPQLVIERT HPDDRASVKE IIDEAMRDLR DFEHEYRLLL PDGSVKHIHA QARVTRTASG
EIEFVGAATD ITAARRAEQQ LRRSEAYLAE AQHLTHTGSW SWDVHTRDFV YRSAEVDRLF
GFNPQEPVSL ETIRSRIHPE DLPGLQEVQR QAIDQEHERF EYDFRVILPD GGIRRIHSVA
HVVVGSDGNV SELIGTHMDV TEQHAARERL ENTLVALRES EQRFRDYAET ASDWLWETGP
DHRVTHLSEH TSAAGILATG LTGLLRWDIA CDMEEEPEKW RQHRATLQAH LPFRDLIYRT
VNRMGSPIYV RTSGKPFFDG NGNFLGYRGV STDITATIRA DQAEQELRKA QAELAHVTRV
TTLGEMTTSI AHEITQPLAA ILSNADACLG WMARDVPNLA AARSSVEWII EDAIRASEVI
RSIRALAKKG EIEMVPLDIN QVVRDVSALV TRELVSHQVT LRSELASALP RVLGDRIQLQ
QVIINLVMNG IEAMDAVTDR PRELLIQSST DDLGYVQLSV TDCGVGIAEN DADRVLDPFF
TTKSSGLGMG LSICRSIVEV HGGRISVVQK NGPGATFQFA LPLHKEAIS
