NODO_RHILV
ID NODO_RHILV Reviewed; 284 AA.
AC P15728;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Nodulation protein O;
GN Name=nodO; Synonyms=nolR;
OS Rhizobium leguminosarum bv. viciae.
OG Plasmid sym pRL1JI.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=387;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-8.
RC STRAIN=8401;
RX PubMed=2303029; DOI=10.1002/j.1460-2075.1990.tb08117.x;
RA Economou A., Hamilton W.D.O., Johnston A.W.B., Downie J.A.;
RT "The Rhizobium nodulation gene nodO encodes a Ca2(+)-binding protein that
RT is exported without N-terminal cleavage and is homologous to haemolysin and
RT related proteins.";
RL EMBO J. 9:349-354(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 4-18.
RX PubMed=2687250; DOI=10.1128/jb.171.12.6764-6770.1989;
RA de Maagd R.A., Wijfjes A.H.M., Spaink H.P., Ruiz-Sainz J.E.,
RA Wijffelman C.A., Okker R.J.H., Lugtenberg B.J.J.;
RT "nodO, a new nod gene of the Rhizobium leguminosarum biovar viciae sym
RT plasmid pRL1JI, encodes a secreted protein.";
RL J. Bacteriol. 171:6764-6770(1989).
CC -!- FUNCTION: The NodO protein may play a role in nodule development by
CC direct interaction with the root hair cells or some other plant surface
CC in a calcium-dependent manner.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=By a mechanism that does not
CC involve an N-terminal signal peptide.
CC -!- INDUCTION: By naringenin (flavonoid).
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DR EMBL; X17285; CAA35178.1; -; Genomic_DNA.
DR EMBL; M29532; AAA26341.1; -; Genomic_DNA.
DR PIR; A43721; A43721.
DR PIR; S08385; S08385.
DR RefSeq; WP_011654216.1; NZ_WIFB01000040.1.
DR AlphaFoldDB; P15728; -.
DR SMR; P15728; -.
DR OMA; ANHAHAF; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR Gene3D; 2.150.10.10; -; 2.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR Pfam; PF00353; HemolysinCabind; 3.
DR SUPFAM; SSF51120; SSF51120; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Metal-binding; Nodulation; Plasmid;
KW Repeat; Secreted.
FT CHAIN 1..284
FT /note="Nodulation protein O"
FT /id="PRO_0000096911"
FT REPEAT 13..30
FT /note="Hemolysin-type calcium-binding 1"
FT REPEAT 31..48
FT /note="Hemolysin-type calcium-binding 2"
FT REPEAT 58..75
FT /note="Hemolysin-type calcium-binding 3"
FT REPEAT 94..111
FT /note="Hemolysin-type calcium-binding 4"
FT REPEAT 112..129
FT /note="Hemolysin-type calcium-binding 5"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..222
FT /note="Export signal (aspartic acid box)"
FT /evidence="ECO:0000255"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:2303029"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:2303029"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:2303029"
FT BINDING 127
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:2303029"
SQ SEQUENCE 284 AA; 30002 MW; 9CA41DCFCBDF8E15 CRC64;
MNIKGSDNGS FIKGSPENDI IDGGKKNDWI DAGNGDDRIK AGDGQDSITA GPGHDIVWAG
KGSDVIHADG GDDLLYSDAS YPLYVTDPHR VIPHSGEGDD VLYAGPGSDI LVAGDGADVL
TGGDDGDAFV FRFHDPMVGT THCYTSVMDF DTKQDRFVLD AADFGGDRNL FDANFINHSK
GFPGEFVDTF YNGAAEGAHG EHVVVITDRG FASAAAAATA IDHEARGDII VFHDQKTLGQ
DGETHGATLA YVDSANHAHA FAHVDNLHDM SDLTSLTAEN FGFI