ID MTSA_STRP1 Reviewed; 310 AA.
AC P0A4G4; Q490I2; Q9A157; Q9RNI7; Q9RNJ0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 134.
DE RecName: Full=Iron ABC transporter substrate-binding lipoprotein MtsA {ECO:0000305};
DE Flags: Precursor;
GN Name=mtsA; OrderedLocusNames=SPy_0453, M5005_Spy0368;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 30-39, AND FUNCTION.
RC STRAIN=AP1 / Serotype M1, and ATCC 700294 / SF370 / Serotype M1;
RX PubMed=10564500; DOI=10.1046/j.1365-2958.1999.01626.x;
RA Janulczyk R., Pallon J., Bjoerck L.;
RT "Identification and characterization of a Streptococcus pyogenes ABC
RT transporter with multiple specificity for metal cations.";
RL Mol. Microbiol. 34:596-606(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(2005).
RN [4] {ECO:0007744|PDB:3HH8}
RP X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 22-310 IN COMPLEX WITH IRON,
RP FUNCTION, AND MUTAGENESIS OF HIS-68; HIS-140; GLU-206 AND ASP-281.
RX PubMed=19463017; DOI=10.1021/bi900552c;
RA Sun X., Baker H.M., Ge R., Sun H., He Q.Y., Baker E.N.;
RT "Crystal structure and metal binding properties of the lipoprotein MtsA,
RT responsible for iron transport in Streptococcus pyogenes.";
RL Biochemistry 48:6184-6190(2009).
CC -!- FUNCTION: Part of the ATP-binding cassette (ABC) transport system
CC MtsABC involved in iron import (PubMed:10564500, PubMed:19463017).
CC Binds iron with high affinity and specificity and delivers it to the
CC membrane permease for translocation into the cytoplasm
CC (PubMed:19463017). Has low affinity for Zn(2+) and Cu(2+)
CC (PubMed:10564500). {ECO:0000269|PubMed:10564500,
CC ECO:0000269|PubMed:19463017}.
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=AAZ50986.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF180520; AAD56936.1; -; Genomic_DNA.
DR EMBL; AF180521; AAD56939.1; -; Genomic_DNA.
DR EMBL; AE004092; AAK33468.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ50986.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_268747.1; NC_002737.2.
DR PDB; 3HH8; X-ray; 1.87 A; A=22-310.
DR PDBsum; 3HH8; -.
DR AlphaFoldDB; P0A4G4; -.
DR SMR; P0A4G4; -.
DR TCDB; 3.A.1.15.6; the atp-binding cassette (abc) superfamily.
DR PaxDb; 1314-HKU360_00400; -.
DR KEGG; spy:SPy_0453; -.
DR KEGG; spz:M5005_Spy0368; -.
DR PATRIC; fig|160490.10.peg.382; -.
DR HOGENOM; CLU_016838_1_1_9; -.
DR OMA; DPHIWFD; -.
DR EvolutionaryTrace; P0A4G4; -.
DR Proteomes; UP000000750; 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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Ion transport;
KW Iron; Iron transport; Lipoprotein; Membrane; Metal-binding; Palmitate;
KW Reference proteome; 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_0000031894"
FT BINDING 68
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000269|PubMed:19463017,
FT ECO:0007744|PDB:3HH8"
FT BINDING 140
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000269|PubMed:19463017,
FT ECO:0007744|PDB:3HH8"
FT BINDING 206
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000269|PubMed:19463017,
FT ECO:0007744|PDB:3HH8"
FT BINDING 281
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000269|PubMed:19463017,
FT ECO:0007744|PDB:3HH8"
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"
FT VARIANT 77
FT /note="V -> A (in strain: AP1)"
FT MUTAGEN 68
FT /note="H->A: 46-fold decrease in affinity for Fe(2+). 100-
FT fold decrease in affinity for Fe(2+); when associated with
FT A-140, A-206 and A-281."
FT /evidence="ECO:0000269|PubMed:19463017"
FT MUTAGEN 140
FT /note="H->A: 60-fold decrease in affinity for Fe(2+). 100-
FT fold decrease in affinity for Fe(2+); when associated with
FT A-68, A-206 and A-281."
FT /evidence="ECO:0000269|PubMed:19463017"
FT MUTAGEN 206
FT /note="E->A: 1.5-fold decrease in affinity for Fe(2+). 100-
FT fold decrease in affinity for Fe(2+); when associated with
FT A-68, A-140 and A-281."
FT /evidence="ECO:0000269|PubMed:19463017"
FT MUTAGEN 281
FT /note="D->A: 18-fold decrease in affinity for Fe(2+). 100-
FT fold decrease in affinity for Fe(2+); when associated with
FT A-68, A-140 and A-206."
FT /evidence="ECO:0000269|PubMed:19463017"
FT CONFLICT 26
FT /note="T -> A (in Ref. 1; AAD56936/AAD56939)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="K -> E (in Ref. 1; AAD56936)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="A -> G (in Ref. 1; AAD56936)"
FT /evidence="ECO:0000305"
FT CONFLICT 49..50
FT /note="AI -> VM (in Ref. 1; AAD56936)"
FT /evidence="ECO:0000305"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:3HH8"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:3HH8"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:3HH8"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:3HH8"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:3HH8"
FT HELIX 74..82
FT /evidence="ECO:0007829|PDB:3HH8"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:3HH8"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:3HH8"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:3HH8"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:3HH8"
FT TURN 119..122
FT /evidence="ECO:0007829|PDB:3HH8"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:3HH8"
FT HELIX 145..162
FT /evidence="ECO:0007829|PDB:3HH8"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:3HH8"
FT HELIX 167..190
FT /evidence="ECO:0007829|PDB:3HH8"
FT TURN 191..194
FT /evidence="ECO:0007829|PDB:3HH8"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:3HH8"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:3HH8"
FT HELIX 210..216
FT /evidence="ECO:0007829|PDB:3HH8"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:3HH8"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:3HH8"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:3HH8"
FT HELIX 261..270
FT /evidence="ECO:0007829|PDB:3HH8"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:3HH8"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:3HH8"
FT HELIX 293..308
FT /evidence="ECO:0007829|PDB:3HH8"
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
//
