MTSA_STRP6
ID MTSA_STRP6 Reviewed; 310 AA.
AC Q5XDI6;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Metal ABC transporter substrate-binding lipoprotein;
DE Flags: Precursor;
GN Name=mtsA; OrderedLocusNames=M6_Spy0392;
OS Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=286636;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-946 / MGAS10394;
RX PubMed=15272401; DOI=10.1086/422697;
RA Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT "Progress toward characterization of the group A Streptococcus metagenome:
RT complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL J. Infect. Dis. 190:727-738(2004).
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=AAT86527.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000003; AAT86527.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011017446.1; NC_006086.1.
DR AlphaFoldDB; Q5XDI6; -.
DR SMR; Q5XDI6; -.
DR EnsemblBacteria; AAT86527; AAT86527; M6_Spy0392.
DR GeneID; 57852190; -.
DR KEGG; spa:M6_Spy0392; -.
DR HOGENOM; CLU_016838_1_1_9; -.
DR OMA; HHVFGYL; -.
DR Proteomes; UP000001167; 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_0000031896"
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; 34330 MW; 40F613659AAD1768 CRC64;
MGKKMSLILG 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