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 27-MAR-2024, entry version 107. DE RecName: Full=Methionine-binding lipoprotein MetQ; DE Flags: Precursor; GN Name=metQ; Synonyms=yusA; OrderedLocusNames=BSU32730; OS Bacillus subtilis (strain 168). OC Bacteria; Bacillota; 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}. 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; 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; 224308-BSU32730; -. 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 OrthoDB; 9812878at2; -. DR PhylomeDB; O32167; -. DR BioCyc; BSUB:BSU32730-MONOMER; -. 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 CDD; cd13597; PBP2_lipoprotein_Tp32; 1. DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2. DR InterPro; IPR004872; Lipoprotein_NlpA. DR PANTHER; PTHR30429; D-METHIONINE-BINDING LIPOPROTEIN METQ; 1. DR PANTHER; PTHR30429:SF0; METHIONINE-BINDING LIPOPROTEIN METQ; 1. DR Pfam; PF03180; Lipoprotein_9; 1. DR PIRSF; PIRSF002854; MetQ; 1. DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 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 //