YXKI_BACSU
ID YXKI_BACSU Reviewed; 562 AA.
AC P94362; Q794Y0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Putative membrane metalloprotease YxkI;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=yxkI; OrderedLocusNames=BSU38780;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BGSC1A1;
RX PubMed=8969509; DOI=10.1099/13500872-142-11-3113;
RA Yoshida K., Shindo K., Sano H., Seki S., Fujimura M., Yanai N., Miwa Y.,
RA Fujita Y.;
RT "Sequencing of a 65 kb region of the Bacillus subtilis genome containing
RT the lic and cel loci, and creation of a 177 kb contig covering the gnt-
RT sacXY region.";
RL Microbiology 142:3113-3123(1996).
RN [2]
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).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase M48 family. {ECO:0000305}.
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DR EMBL; D83026; BAA11725.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15904.1; -; Genomic_DNA.
DR PIR; B70081; B70081.
DR RefSeq; NP_391757.1; NC_000964.3.
DR RefSeq; WP_010886639.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P94362; -.
DR STRING; 224308.BSU38780; -.
DR MEROPS; M48.A11; -.
DR PaxDb; P94362; -.
DR PRIDE; P94362; -.
DR EnsemblBacteria; CAB15904; CAB15904; BSU_38780.
DR GeneID; 937415; -.
DR KEGG; bsu:BSU38780; -.
DR PATRIC; fig|224308.43.peg.4064; -.
DR eggNOG; COG0501; Bacteria.
DR OMA; HEAIHIK; -.
DR BioCyc; BSUB:BSU38780-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR001915; Peptidase_M48.
DR Pfam; PF01435; Peptidase_M48; 1.
PE 3: Inferred from homology;
KW Cell membrane; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Zinc.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..562
FT /note="Putative membrane metalloprotease YxkI"
FT /id="PRO_0000379981"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 390
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 457
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 562 AA; 63612 MW; F14B4F3EBDB2C68D CRC64;
MPMGTHLFLF MLLGLGFYLI SALAAKLIPA IDFWIDIVLW VGAAAYIFSH LSFMDGIVSL
ATMFYCYWTA MDLIVSERVE KPSGDWQEIE LAKNKTRLLS DITLTAIVFA GAVIFFIYGP
DTSPLKYVIL LGMISGGGAL VKRILNVFSV KVFYSAALEK LHISSHYETR TYPLSDLKNI
QLESTADLLK LHPLLTMYSS RLDLTTSFQQ VIKLSLPGET LFLTVKEPQK WKTILQEYTD
AENNVDNVIS VLPFYHRKNV KRLLGKLYFA ASVKGVSAYA LLVLALYALH ASPWVMAVAV
ILYWVFNMYM SDRVLRAAMD AKSCHHPHVQ AAADKIFRSA GISHVRIYET ESDDYNGMAV
GMNVGRSMVI LTSATLTLPQ RVIEGILAHE AIHIKKRDVL SSQLLRFLYL GAVVGIFLLF
EQHITHPEAH KIALWAFIMA IIILFQLYQS FCSQWMEVRA DNLGASLLDG GYKQMAEALR
ILAVRQDEDI QKQSAYSSEA GEDELQIDSL TRDKSWFFRL IDFQFAPHPP MYWRVGTLLS
NKGHGVLKRW LRDRLKESIT LK
