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MLTG_BACSU
ID   MLTG_BACSU              Reviewed;         360 AA.
AC   O34758;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Endolytic murein transglycosylase {ECO:0000255|HAMAP-Rule:MF_02065};
DE            EC=4.2.2.- {ECO:0000255|HAMAP-Rule:MF_02065};
DE   AltName: Full=Peptidoglycan polymerization terminase {ECO:0000255|HAMAP-Rule:MF_02065};
GN   Name=mltG {ECO:0000255|HAMAP-Rule:MF_02065}; Synonyms=yrrL;
GN   OrderedLocusNames=BSU27370;
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).
CC   -!- FUNCTION: Functions as a peptidoglycan terminase that cleaves nascent
CC       peptidoglycan strands endolytically to terminate their elongation.
CC       {ECO:0000255|HAMAP-Rule:MF_02065}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_02065};
CC       Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02065}.
CC   -!- SIMILARITY: Belongs to the transglycosylase MltG family.
CC       {ECO:0000255|HAMAP-Rule:MF_02065}.
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DR   EMBL; AL009126; CAB14679.1; -; Genomic_DNA.
DR   PIR; E69979; E69979.
DR   RefSeq; NP_390615.1; NC_000964.3.
DR   RefSeq; WP_003229799.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O34758; -.
DR   SMR; O34758; -.
DR   STRING; 224308.BSU27370; -.
DR   PaxDb; O34758; -.
DR   PRIDE; O34758; -.
DR   EnsemblBacteria; CAB14679; CAB14679; BSU_27370.
DR   GeneID; 936260; -.
DR   KEGG; bsu:BSU27370; -.
DR   PATRIC; fig|224308.179.peg.2973; -.
DR   eggNOG; COG1559; Bacteria.
DR   InParanoid; O34758; -.
DR   OMA; IAMPGKA; -.
DR   PhylomeDB; O34758; -.
DR   BioCyc; BSUB:BSU27370-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008932; F:lytic endotransglycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd08010; MltG_like; 1.
DR   HAMAP; MF_02065; MltG; 1.
DR   InterPro; IPR003770; MLTG-like.
DR   PANTHER; PTHR30518; PTHR30518; 1.
DR   Pfam; PF02618; YceG; 1.
DR   TIGRFAMs; TIGR00247; TIGR00247; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cell wall biogenesis/degradation; Lyase; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..360
FT                   /note="Endolytic murein transglycosylase"
FT                   /id="PRO_0000388727"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02065"
FT   SITE            242
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02065"
SQ   SEQUENCE   360 AA;  40502 MW;  4EFDC5CC9B0588C3 CRC64;
     MYINQQKKSF FNKKRIILSS IVVLFLIIGG AFLYGKSLLE PVEKDSKTTV NINIPSGSSV
     SAIASILKKN DVIKSEKAFQ YYVKYKGASG FQAGFYHLNK GMDLDAIIQK LTSGATGYAF
     QITVTEGAQL TQIAAAIADE TKYSKKQVIA KLDDETFINQ LKKEFPDTVT NDVFNKNIKH
     PLEGYLFPAT YPFNDPDTSL EDIIKAMIKQ TNSYVETYKS EMKKNKVSVH KLLTMASLIE
     EEATEKADRH KIASVFYNRL KKKMPLQTDP TVLYAAGKHK DRVLYKDLEI DSPYNTYKNT
     GLTPGPIANA GMSSWEAALH PDKTDYLYFL AKSNGEVVFT KTLKEHNKAK EKYISSKNEK
 
 
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