METQ_BACSU
ID METQ_BACSU Reviewed; 274 AA.
AC O32167;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Methionine-binding lipoprotein MetQ;
DE Flags: Precursor;
GN Name=metQ; Synonyms=yusA; OrderedLocusNames=BSU32730;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP PROBABLE FUNCTION IN METHIONINE AND METHIONINE SULFOXIDE TRANSPORT, AND
RP INDUCTION.
RC STRAIN=168;
RX PubMed=14990259; DOI=10.1016/j.resmic.2003.11.008;
RA Hullo M.-F., Auger S., Dassa E., Danchin A., Martin-Verstraete I.;
RT "The metNPQ operon of Bacillus subtilis encodes an ABC permease
RT transporting methionine sulfoxide, D- and L-methionine.";
RL Res. Microbiol. 155:80-86(2004).
CC -!- FUNCTION: Part of the ABC transporter complex MetNPQ involved in
CC methionine import. Binds the methionine and transfers it to the
CC membrane-bound permease. It has also been shown to be involved in
CC methionine sulfoxide transport (Probable). {ECO:0000305}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (MetN),
CC two transmembrane proteins (MetP) and a solute-binding protein (metQ).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- INDUCTION: Repressed by methionine via the S-box system.
CC {ECO:0000269|PubMed:14990259}.
CC -!- SIMILARITY: Belongs to the NlpA lipoprotein family. {ECO:0000305}.
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DR EMBL; AL009126; CAB15262.1; -; Genomic_DNA.
DR PIR; B70020; B70020.
DR RefSeq; NP_391152.1; NC_000964.3.
DR RefSeq; WP_003228595.1; NZ_JNCM01000033.1.
DR PDB; 4GOT; X-ray; 1.95 A; A=27-274.
DR PDBsum; 4GOT; -.
DR AlphaFoldDB; O32167; -.
DR SMR; O32167; -.
DR STRING; 224308.BSU32730; -.
DR TCDB; 3.A.1.24.2; the atp-binding cassette (abc) superfamily.
DR jPOST; O32167; -.
DR PaxDb; O32167; -.
DR PRIDE; O32167; -.
DR DNASU; 936716; -.
DR EnsemblBacteria; CAB15262; CAB15262; BSU_32730.
DR GeneID; 936716; -.
DR KEGG; bsu:BSU32730; -.
DR PATRIC; fig|224308.179.peg.3546; -.
DR eggNOG; COG1464; Bacteria.
DR InParanoid; O32167; -.
DR OMA; HIEPMGV; -.
DR PhylomeDB; O32167; -.
DR BioCyc; BSUB:BSU32730-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR InterPro; IPR004872; Lipoprotein_NlpA.
DR PANTHER; PTHR30429; PTHR30429; 1.
DR Pfam; PF03180; Lipoprotein_9; 1.
DR PIRSF; PIRSF002854; MetQ; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid transport; Cell membrane; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 20..274
FT /note="Methionine-binding lipoprotein MetQ"
FT /id="PRO_0000383645"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:4GOT"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:4GOT"
FT HELIX 42..54
FT /evidence="ECO:0007829|PDB:4GOT"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:4GOT"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:4GOT"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:4GOT"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:4GOT"
FT HELIX 88..97
FT /evidence="ECO:0007829|PDB:4GOT"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:4GOT"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:4GOT"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:4GOT"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:4GOT"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:4GOT"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:4GOT"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:4GOT"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:4GOT"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:4GOT"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:4GOT"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:4GOT"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:4GOT"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:4GOT"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:4GOT"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:4GOT"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:4GOT"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:4GOT"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:4GOT"
FT HELIX 255..264
FT /evidence="ECO:0007829|PDB:4GOT"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:4GOT"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:4GOT"
SQ SEQUENCE 274 AA; 30355 MW; 3D40F949A1BFC73C CRC64;
MKKLFLGALL LVFAGVMAAC GSNNGAESGK KEIVVAATKT PHAEILKEAE PLLKEKGYTL
KVKVLSDYKM YNKALADKEV DANYFQHIPY LEQEMKENTD YKLVNAGAVH LEPFGIYSKT
YKSLKDLPDG ATIILTNNVA EQGRMLAMLE NAGLITLDSK VETVDATLKD IKKNPKNLEF
KKVAPELTAK AYENKEGDAV FINVNYAIQN KLNPKKDAIE VESTKNNPYA NIIAVRKGEE
DSAKIKALME VLHSKKIKDF IEKKYDGAVL PVSE
