SMBP_NITEU
ID SMBP_NITEU Reviewed; 117 AA.
AC Q82S91;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Metal-binding protein SmbP;
DE Flags: Precursor;
GN Name=smbP; OrderedLocusNames=NE2461;
OS Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS 14298).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=228410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003;
RA Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT chemolithoautotroph Nitrosomonas europaea.";
RL J. Bacteriol. 185:2759-2773(2003).
RN [2]
RP PROTEIN SEQUENCE OF 25-35, CHARACTERIZATION, SUBUNIT, SUBCELLULAR LOCATION,
RP TRANSCRIPTIONAL REGULATION, AND MASS SPECTROMETRY.
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=15366930; DOI=10.1021/bi049318k;
RA Barney B.M., LoBrutto R., Francisco W.A.;
RT "Characterization of a small metal binding protein from Nitrosomonas
RT europaea.";
RL Biochemistry 43:11206-11213(2004).
CC -!- FUNCTION: Is capable of binding multiple equivalents of a variety of
CC divalent and trivalent metals, including Cu(2+) and Fe(3+) but also
CC Mn(2+), Ni(2+), Mg(2+) and Zn(2+). Is able to bind up to six Cu(2+)
CC atoms. It is proposed to be a metal scavenging protein that has a role
CC in cellular copper management in N.europaea.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15366930}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:15366930}.
CC -!- INDUCTION: By copper. {ECO:0000269|PubMed:15366930}.
CC -!- MASS SPECTROMETRY: Mass=9866; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15366930};
CC -!- MISCELLANEOUS: There are two separate and distinct copper binding
CC sites, a high-affinity site and a lower affinity site, which display
CC negative cooperativity.
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DR EMBL; AL954747; CAD86373.1; -; Genomic_DNA.
DR RefSeq; WP_011112924.1; NC_004757.1.
DR PDB; 3U8V; X-ray; 1.90 A; A/B=25-117.
DR PDBsum; 3U8V; -.
DR AlphaFoldDB; Q82S91; -.
DR SMR; Q82S91; -.
DR STRING; 228410.NE2461; -.
DR EnsemblBacteria; CAD86373; CAD86373; NE2461.
DR KEGG; neu:NE2461; -.
DR eggNOG; ENOG50334TW; Bacteria.
DR HOGENOM; CLU_130934_1_1_4; -.
DR OMA; TKHAQEA; -.
DR OrthoDB; 2092042at2; -.
DR Proteomes; UP000001416; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd13840; SMBP_like; 1.
DR DisProt; DP00205; -.
DR InterPro; IPR031877; SmbP.
DR Pfam; PF16785; SMBP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Direct protein sequencing; Metal-binding; Periplasm;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:15366930"
FT CHAIN 25..117
FT /note="Metal-binding protein SmbP"
FT /id="PRO_0000227659"
FT REPEAT 27..33
FT /note="1"
FT REPEAT 34..40
FT /note="2"
FT REPEAT 41..47
FT /note="3"
FT REPEAT 53..59
FT /note="4"
FT REPEAT 60..66
FT /note="5"
FT REPEAT 72..78
FT /note="6"
FT REPEAT 79..85
FT /note="7"
FT REPEAT 86..92
FT /note="8"
FT REPEAT 98..104
FT /note="9"
FT REPEAT 105..111
FT /note="10"
FT REGION 27..111
FT /note="10 X 7 AA approximate repeats"
FT HELIX 27..46
FT /evidence="ECO:0007829|PDB:3U8V"
FT HELIX 50..67
FT /evidence="ECO:0007829|PDB:3U8V"
FT HELIX 75..91
FT /evidence="ECO:0007829|PDB:3U8V"
FT HELIX 95..111
FT /evidence="ECO:0007829|PDB:3U8V"
SQ SEQUENCE 117 AA; 12448 MW; 1275976B6114414C CRC64;
MKTTLIKVIA ASVTALFLSM QVYASGHTAH VDEAVKHAEE AVAHGKEGHT DQLLEHAKES
LTHAKAASEA GGNTHVGHGI KHLEDAIKHG EEGHVGVATK HAQEAIEHLR ASEHKSH