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COMER_BACSU
ID   COMER_BACSU             Reviewed;         273 AA.
AC   P39696;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   24-OCT-2003, sequence version 3.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=ComE operon protein 4;
GN   Name=comER; Synonyms=comE4, comED; OrderedLocusNames=BSU25600;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7968523; DOI=10.1111/j.1365-2958.1993.tb00907.x;
RA   Hahn J., Inamine G., Kozlov Y., Dubnau D.A.;
RT   "Characterization of comE, a late competence operon of Bacillus subtilis
RT   required for the binding and uptake of transforming DNA.";
RL   Mol. Microbiol. 10:99-110(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [3]
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   [4]
RP   POSSIBLE FUNCTION.
RX   PubMed=11418582; DOI=10.1128/jb.183.14.4389-4392.2001;
RA   Belitsky B.R., Brill J., Bremer E., Sonenshein A.L.;
RT   "Multiple genes for the last step of proline biosynthesis in Bacillus
RT   subtilis.";
RL   J. Bacteriol. 183:4389-4392(2001).
CC   -!- FUNCTION: Dispensable for transformability. Not known if it can act as
CC       a pyrroline-5-carboxylate reductase.
CC   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC36904.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L15202; AAC36904.1; ALT_INIT; Unassigned_DNA.
DR   EMBL; D84432; BAA12451.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14502.1; -; Genomic_DNA.
DR   PIR; F69602; F69602.
DR   RefSeq; NP_390438.1; NC_000964.3.
DR   RefSeq; WP_004398597.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P39696; -.
DR   SMR; P39696; -.
DR   STRING; 224308.BSU25600; -.
DR   PaxDb; P39696; -.
DR   PRIDE; P39696; -.
DR   DNASU; 937834; -.
DR   EnsemblBacteria; CAB14502; CAB14502; BSU_25600.
DR   GeneID; 937834; -.
DR   KEGG; bsu:BSU25600; -.
DR   PATRIC; fig|224308.179.peg.2783; -.
DR   eggNOG; COG0345; Bacteria.
DR   OMA; VSCGPAF; -.
DR   PhylomeDB; P39696; -.
DR   BioCyc; BSUB:BSU25600-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IBA:GO_Central.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR028939; P5C_Rdtase_cat_N.
DR   InterPro; IPR029036; P5CR_dimer.
DR   InterPro; IPR000304; Pyrroline-COOH_reductase.
DR   PANTHER; PTHR11645; PTHR11645; 1.
DR   Pfam; PF03807; F420_oxidored; 1.
DR   Pfam; PF14748; P5CR_dimer; 1.
DR   PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00521; P5CR; 1.
PE   3: Inferred from homology;
KW   Reference proteome.
FT   CHAIN           1..273
FT                   /note="ComE operon protein 4"
FT                   /id="PRO_0000187330"
FT   CONFLICT        153..154
FT                   /note="HP -> QA (in Ref. 1; AAC36904)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   273 AA;  30239 MW;  9E72F798B4EB3F60 CRC64;
     MKIGFIGTGN MGTILIESFI ESKAADPSNM TITNRTIEKA LHIKNRYNSI NVTESLEKLV
     SENEMIFICV KPLDIYPLLA RALPYLRKDH ILISITSPVQ TEQLEQYVPC QVARVIPSIT
     NRALAGVSLV TFGTSCGESA KAKINELMQH ISHPLQIESD ITRVASDIVS CGPAFMSYLI
     QRFIDAAVSE TSVSKQDAIL MCKEMLVGMG KLLETELYTL PALQEKVCVK GGVTGEGIKA
     LESGVQDMFH RVFQNTHMKY EEDISAVKKQ FHV
 
 
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