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LIPC_BACLD
ID   LIPC_BACLD              Reviewed;         212 AA.
AC   Q65NA4; Q62YQ6;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Spore germination lipase LipC;
DE            EC=3.-.-.-;
GN   Name=lipC; Synonyms=ycsK; OrderedLocusNames=BLi00504, BL02812;
OS   Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS   NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15383718; DOI=10.1159/000079829;
RA   Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA   Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT   "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT   with great industrial potential.";
RL   J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA   Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA   Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:R77.1-R77.12(2004).
CC   -!- FUNCTION: Lipase involved in spore germination. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Spore coat {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AE017333; AAU39460.1; -; Genomic_DNA.
DR   EMBL; CP000002; AAU22102.1; -; Genomic_DNA.
DR   RefSeq; WP_011197556.1; NC_006322.1.
DR   PDB; 6NKD; X-ray; 2.80 A; A/B=1-212.
DR   PDBsum; 6NKD; -.
DR   AlphaFoldDB; Q65NA4; -.
DR   SMR; Q65NA4; -.
DR   STRING; 279010.BL02812; -.
DR   EnsemblBacteria; AAU22102; AAU22102; BL02812.
DR   GeneID; 66217345; -.
DR   KEGG; bld:BLi00504; -.
DR   KEGG; bli:BL02812; -.
DR   eggNOG; COG2755; Bacteria.
DR   HOGENOM; CLU_076859_3_0_9; -.
DR   OMA; LYNPFPG; -.
DR   OrthoDB; 1247435at2; -.
DR   BioCyc; BLIC279010:BLI_RS02485-MON; -.
DR   Proteomes; UP000000606; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1110; -; 1.
DR   InterPro; IPR013830; SGNH_hydro.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   Pfam; PF13472; Lipase_GDSL_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Reference proteome; Sporulation.
FT   CHAIN           1..212
FT                   /note="Spore germination lipase LipC"
FT                   /id="PRO_0000281677"
FT   ACT_SITE        11
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        186
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        189
FT                   /evidence="ECO:0000250"
FT   BINDING         50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   STRAND          3..10
FT                   /evidence="ECO:0007829|PDB:6NKD"
FT   HELIX           11..14
FT                   /evidence="ECO:0007829|PDB:6NKD"
FT   TURN            15..17
FT                   /evidence="ECO:0007829|PDB:6NKD"
FT   HELIX           25..37
FT                   /evidence="ECO:0007829|PDB:6NKD"
FT   STRAND          41..47
FT                   /evidence="ECO:0007829|PDB:6NKD"
FT   HELIX           53..59
FT                   /evidence="ECO:0007829|PDB:6NKD"
FT   HELIX           63..71
FT                   /evidence="ECO:0007829|PDB:6NKD"
FT   STRAND          73..77
FT                   /evidence="ECO:0007829|PDB:6NKD"
FT   HELIX           81..94
FT                   /evidence="ECO:0007829|PDB:6NKD"
FT   HELIX           98..122
FT                   /evidence="ECO:0007829|PDB:6NKD"
FT   STRAND          130..134
FT                   /evidence="ECO:0007829|PDB:6NKD"
FT   HELIX           144..157
FT                   /evidence="ECO:0007829|PDB:6NKD"
FT   HELIX           158..160
FT                   /evidence="ECO:0007829|PDB:6NKD"
FT   TURN            163..165
FT                   /evidence="ECO:0007829|PDB:6NKD"
FT   STRAND          166..169
FT                   /evidence="ECO:0007829|PDB:6NKD"
FT   HELIX           171..175
FT                   /evidence="ECO:0007829|PDB:6NKD"
FT   HELIX           179..182
FT                   /evidence="ECO:0007829|PDB:6NKD"
FT   STRAND          187..190
FT                   /evidence="ECO:0007829|PDB:6NKD"
FT   HELIX           192..204
FT                   /evidence="ECO:0007829|PDB:6NKD"
FT   HELIX           208..210
FT                   /evidence="ECO:0007829|PDB:6NKD"
SQ   SEQUENCE   212 AA;  24123 MW;  9DD32290A5E29415 CRC64;
     MTLQYTALGD SLTVGVGAGL FEPGFVQRYK RKMEEDLNEE VSLIVFAKSG LETSEILAML
     NEPFIMEQVK KADVITITGC GNDLLQSLEI YEKEKDEHVF LEASSHCQKN YSGMLEKIRE
     IKGEKDTRYL VRLLNLYNPF PSIELADKWI SGFNRHLKQL ESAPQIKVID TYAVFKGREK
     EYLSIDRVHP SSRGYEAMSE KLRAAGYGRL EG
 
 
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