ID   NSPS_VIBCH              Reviewed;         359 AA.
AC   Q9KU25;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Norspermidine sensor;
DE   AltName: Full=Norspermidine-binding protein;
DE   Flags: Precursor;
GN   Name=nspS; OrderedLocusNames=VC_0704;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=MO10 / Serotype O139;
RX   PubMed=16237027; DOI=10.1128/jb.187.21.7434-7443.2005;
RA   Karatan E., Duncan T.R., Watnick P.I.;
RT   "NspS, a predicted polyamine sensor, mediates activation of Vibrio cholerae
RT   biofilm formation by norspermidine.";
RL   J. Bacteriol. 187:7434-7443(2005).
CC   -!- FUNCTION: Acts as a sensor of norspermidine and enhances biofilm
CC       formation. When complexed to norspermidine, could interact with the
CC       periplasmic portion of MbaA to regulate its enzymatic activity.
CC       {ECO:0000269|PubMed:16237027}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutants form biofilms thinner than
CC       wild- type and show greatly reduced surface accumulation compared to
CC       wild-type. {ECO:0000269|PubMed:16237027}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein PotD/PotF
CC       family. {ECO:0000305}.
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DR   EMBL; AE003852; AAF93869.1; -; Genomic_DNA.
DR   PIR; B82291; B82291.
DR   RefSeq; NP_230353.1; NC_002505.1.
DR   AlphaFoldDB; Q9KU25; -.
DR   SMR; Q9KU25; -.
DR   STRING; 243277.VC_0704; -.
DR   DNASU; 2615708; -.
DR   EnsemblBacteria; AAF93869; AAF93869; VC_0704.
DR   KEGG; vch:VC_0704; -.
DR   PATRIC; fig|243277.26.peg.674; -.
DR   eggNOG; COG0687; Bacteria.
DR   HOGENOM; CLU_026974_1_3_6; -.
DR   OMA; VLTYEYV; -.
DR   BioCyc; VCHO:VC0704-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0019808; F:polyamine binding; IEA:InterPro.
DR   GO; GO:0015846; P:polyamine transport; IEA:InterPro.
DR   InterPro; IPR006059; SBP.
DR   InterPro; IPR001188; Sperm_putr-bd.
DR   Pfam; PF13416; SBP_bac_8; 1.
DR   PRINTS; PR00909; SPERMDNBNDNG.
PE   3: Inferred from homology;
KW   Periplasm; Reference proteome; Signal; Transport.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..359
FT                   /note="Norspermidine sensor"
FT                   /id="PRO_0000042813"
SQ   SEQUENCE   359 AA;  40899 MW;  CF1B20D6525CE8A7 CRC64;
     MTNFCNEWVS YSQMIKRFLS LMVLNTVCYQ ASALELNVYL WEDTIAPSVV EAWHKKTGVS
     VNLFHFDNDD ERSLLMLKSV QLPFDIMVLD NVSAFIFSRQ NVFEDLTALP NRANNDPMWL
     QACGTHAVPY FWGSVGIAYR KSLFDKPPTQ WSEVVDIAPA HRGRVGMLKD SVETLLPALY
     MLNASPITDS IDTLRQAYRL LDAANPHILT YEYVLSYVRS HPQTDNLHMA VSYSGDHYSL
     NRFFNTQDWD FSVPEGRPYL WVDCMAVNSV SPNTVQAKAF LDFLMKPDIA AINAEYIRAA
     SPNYKARALL PVEHREDLSI YLPEQRLAEG IIDSELSAKN LSLRAKIISS VTYQYEAKP