ID   MTSA_STRP3              Reviewed;         310 AA.
AC   P0DF60; P0A4G5; Q9A157; Q9RNI7; Q9RNJ0;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Metal ABC transporter substrate-binding lipoprotein;
DE   Flags: Precursor;
GN   Name=mtsA; OrderedLocusNames=SpyM3_0318;
OS   Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=198466;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-595 / MGAS315;
RX   PubMed=12122206; DOI=10.1073/pnas.152298499;
RA   Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D.,
RA   Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S.,
RA   Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.;
RT   "Genome sequence of a serotype M3 strain of group A Streptococcus: phage-
RT   encoded toxins, the high-virulence phenotype, and clone emergence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(2002).
CC   -!- FUNCTION: Part of an ATP-driven transport system. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 9 family.
CC       Lipoprotein receptor antigen (Lrai) subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM78925.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014074; AAM78925.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_004218965.1; NC_004070.1.
DR   AlphaFoldDB; P0DF60; -.
DR   SMR; P0DF60; -.
DR   EnsemblBacteria; AAM78925; AAM78925; SpyM3_0318.
DR   KEGG; spg:SpyM3_0318; -.
DR   HOGENOM; CLU_016838_1_1_9; -.
DR   OMA; HHVFGYL; -.
DR   Proteomes; UP000000564; Chromosome.
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:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR   GO; GO:0006829; P:zinc ion transport; IEA:UniProtKB-KW.
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; Copper; Copper transport; Ion transport; Iron;
KW   Iron transport; Lipoprotein; Membrane; Metal-binding; Palmitate; Signal;
KW   Transport; Zinc; Zinc transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           21..310
FT                   /note="Metal ABC transporter substrate-binding lipoprotein"
FT                   /id="PRO_0000031895"
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           21
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           21
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   310 AA;  34358 MW;  B0F829EF1C72CADC CRC64;
     MGKRMSLILG AFLSVFLLVA CSSTGTKTAK SDKLKVVATN SIIADMTKAI AGDKIDLHSI
     VPIGQDPHEY EPLPEDVEKT SNADVIFYNG INLEDGGQAW FTKLVKNAQK TKNKDYFAVS
     DGIDVIYLEG ASEKGKEDPH AWLNLENGII YSKNIAKQLI AKDPKNKETY EKNLKAYVAK
     LEKLDKEAKS KFDAIAENKK LIVTSEGCFK YFSKAYGVPS AYIWEINTEE EGTPDQISSL
     IEKLKVIKPS ALFVESSVDR RPMETVSKDS GIPIYSEIFT DSIAKKGKPG DSYYAMMKWN
     LDKISEGLAK