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}; 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; 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+). FT 100-fold decrease in affinity for Fe(2+); when associated FT with 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+). FT 100-fold decrease in affinity for Fe(2+); when associated FT with 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+). FT 100-fold decrease in affinity for Fe(2+); when associated FT with 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+). FT 100-fold decrease in affinity for Fe(2+); when associated FT with 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 //