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 27-MAR-2024, entry version 58.
DE RecName: Full=Iron ABC transporter substrate-binding lipoprotein MtsA {ECO:0000305};
DE Flags: Precursor;
GN Name=mtsA; OrderedLocusNames=SpyM3_0318;
OS Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315).
OC Bacteria; Bacillota; 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 the ATP-binding cassette (ABC) transport system
CC MtsABC involved in iron import. Binds iron with high affinity and
CC specificity and delivers it to the membrane permease for translocation
CC into the cytoplasm. Has low affinity for Zn(2+) and Cu(2+).
CC {ECO:0000250|UniProtKB:P0A4G4}.
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 GeneID; 69901308; -.
DR KEGG; spg:SpyM3_0318; -.
DR HOGENOM; CLU_016838_1_1_9; -.
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:0006826; P:iron ion transport; IEA:UniProtKB-KW.
DR CDD; cd01137; PsaA; 1.
DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2.
DR InterPro; IPR006129; AdhesinB.
DR InterPro; IPR006128; Lipoprotein_PsaA-like.
DR InterPro; IPR006127; ZnuA-like.
DR NCBIfam; NF040928; ABC_lipo_SloC; 1.
DR PANTHER; PTHR42953; HIGH-AFFINITY ZINC UPTAKE SYSTEM PROTEIN ZNUA-RELATED; 1.
DR PANTHER; PTHR42953:SF1; MANGANESE ABC TRANSPORTER SUBSTRATE-BINDING LIPOPROTEIN; 1.
DR Pfam; PF01297; ZnuA; 1.
DR PRINTS; PR00691; ADHESINB.
DR PRINTS; PR00690; ADHESNFAMILY.
DR SUPFAM; SSF53807; Helical backbone' metal receptor; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell membrane; Ion transport; Iron; Iron transport; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 21..310
FT /note="Iron ABC transporter substrate-binding lipoprotein
FT MtsA"
FT /id="PRO_0000031895"
FT BINDING 68
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000250|UniProtKB:P0A4G4"
FT BINDING 140
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000250|UniProtKB:P0A4G4"
FT BINDING 206
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000250|UniProtKB:P0A4G4"
FT BINDING 281
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000250|UniProtKB:P0A4G4"
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
//
