ID   MTSA_STRCR              Reviewed;         310 AA.
AC   Q53891;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Metal ABC transporter substrate-binding lipoprotein;
DE   Flags: Precursor;
GN   Name=scbA;
OS   Streptococcus cristatus.
OG   Plasmid pSCBA002.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=45634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CC5A;
RX   PubMed=8675315; DOI=10.1128/iai.64.6.2114-2121.1996;
RA   Correia F.F., DiRienzo J.M., McKay T.L., Rosan B.;
RT   "scbA from Streptococcus crista CC5A: an atypical member of the lraI gene
RT   family.";
RL   Infect. Immun. 64:2114-2121(1996).
CC   -!- FUNCTION: Part of an ATP-driven transport system for manganese. Does
CC       not exhibit adhesion properties.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 9 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U46542; AAC44133.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q53891; -.
DR   SMR; Q53891; -.
DR   STRING; 45634.SCRDD08_00258; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0030001; P:metal ion transport; IEA:InterPro.
DR   InterPro; IPR006129; AdhesinB.
DR   InterPro; IPR006128; Lipoprotein_4.
DR   InterPro; IPR006127; ZnuA-like.
DR   Pfam; PF01297; ZnuA; 1.
DR   PRINTS; PR00691; ADHESINB.
DR   PRINTS; PR00690; ADHESNFAMILY.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Lipoprotein; Manganese; Membrane; Metal-binding; Palmitate;
KW   Plasmid; Signal; Transport; Zinc.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000305"
FT   CHAIN           20..310
FT                   /note="Metal ABC transporter substrate-binding lipoprotein"
FT                   /id="PRO_0000031885"
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         281
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   LIPID           20
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000305"
FT   LIPID           20
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   310 AA;  34725 MW;  14D8F7283ECF5936 CRC64;
     MKKCRFLVLL LLAFVGLAAC SSQKSSTETG SSKLNVVATN SIIADITKNI AGDKINLHSI
     VPVGQDPHEY EPLPEDVKKT SQADLIFYNG INLETGGNAW FTKLVENAKK KENKDYYAVS
     EGVDVIYLEG QSEKGKEDPH AWLNLENGII YAQNIAKRLS EKDPANKETY EKNLKAYVEK
     LSALDKEAKE KFNNIPGEKK MIVTSEGCFK YFSKAYNVPS AYIWEINTEE EGTPDQIKTL
     VEKLRKTKVP SLFVESSVDD RPMKTVSKDT NIPIYAKIFT DSVAEKGEEG DSYYSMMKYN
     LEKIAEGLSK