MNTA_LISMO
ID MNTA_LISMO Reviewed; 310 AA.
AC Q8Y653;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Manganese-binding lipoprotein MntA;
DE Flags: Precursor;
GN Name=mntA; OrderedLocusNames=lmo1847;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
CC -!- FUNCTION: This protein is probably a component of a manganese permease,
CC a binding protein-dependent, ATP-driven transport system.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 9 family.
CC {ECO:0000305}.
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DR EMBL; AL591981; CAC99925.1; -; Genomic_DNA.
DR PIR; AG1305; AG1305.
DR RefSeq; NP_465372.1; NC_003210.1.
DR RefSeq; WP_003724071.1; NZ_CP023861.1.
DR PDB; 5HX7; X-ray; 1.75 A; A=24-310.
DR PDB; 5I4K; X-ray; 1.79 A; A=24-310.
DR PDB; 5JPD; X-ray; 1.72 A; A=24-310.
DR PDBsum; 5HX7; -.
DR PDBsum; 5I4K; -.
DR PDBsum; 5JPD; -.
DR AlphaFoldDB; Q8Y653; -.
DR SMR; Q8Y653; -.
DR STRING; 169963.lmo1847; -.
DR PaxDb; Q8Y653; -.
DR EnsemblBacteria; CAC99925; CAC99925; CAC99925.
DR GeneID; 985848; -.
DR KEGG; lmo:lmo1847; -.
DR PATRIC; fig|169963.11.peg.1892; -.
DR eggNOG; COG0803; Bacteria.
DR HOGENOM; CLU_016838_1_1_9; -.
DR OMA; DPHIWFD; -.
DR PhylomeDB; Q8Y653; -.
DR BioCyc; LMON169963:LMO1847-MON; -.
DR Proteomes; UP000000817; 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:0030001; P:metal ion transport; IEA:InterPro.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Lipoprotein; Membrane; Metal-binding;
KW Palmitate; Reference proteome; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 19..310
FT /note="Manganese-binding lipoprotein MntA"
FT /id="PRO_0000031882"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:5JPD"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:5JPD"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:5JPD"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:5JPD"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:5JPD"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:5JPD"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:5JPD"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:5JPD"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:5JPD"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:5JPD"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:5JPD"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:5JPD"
FT TURN 119..122
FT /evidence="ECO:0007829|PDB:5JPD"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:5JPD"
FT HELIX 145..162
FT /evidence="ECO:0007829|PDB:5JPD"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:5JPD"
FT HELIX 167..191
FT /evidence="ECO:0007829|PDB:5JPD"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:5JPD"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:5JPD"
FT HELIX 210..216
FT /evidence="ECO:0007829|PDB:5JPD"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:5JPD"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:5HX7"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:5JPD"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:5JPD"
FT HELIX 261..270
FT /evidence="ECO:0007829|PDB:5JPD"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:5JPD"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:5JPD"
FT HELIX 293..309
FT /evidence="ECO:0007829|PDB:5JPD"
SQ SEQUENCE 310 AA; 34417 MW; E1899348AA68C804 CRC64;
MKKIIVVSLF ALVVVLAGCS SQNSDSKKTD GKLNVVATYS ILADIVKNVG GNKIELHSIV
PVGVDPHEYD PLPANIQSAA DADLIFYNGL NLETGNGWFD RMLETADKSR EDKNQVVELS
KGVKPKYLTE KGKTSETDPH AWLDLHNGII YTENVRDALV KADPDNADFY KENAKKYIDK
LATLDKEAKQ KFADLPENQK TLVTSEGAFK YFAARYGLKA AYIWEINTES QGTPDQMKQI
VGIVEKEKVP NLFVETSVDP RSMESVSKET GVPIFAKIFT DSTAKKGEVG DTYLEMMRYN
LDKIHDGLAK
