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YRHL_BACSU
ID   YRHL_BACSU              Reviewed;         634 AA.
AC   O05402; Q795Y7;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Putative peptidoglycan O-acetyltransferase YrhL;
DE            EC=2.3.1.-;
GN   Name=yrhL; OrderedLocusNames=BSU27140;
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;
RX   PubMed=9308178; DOI=10.1099/00221287-143-9-2939;
RA   Sorokin A., Bolotin A., Purnelle B., Hilbert H., Lauber J.,
RA   Duesterhoeft A., Ehrlich S.D.;
RT   "Sequence of the Bacillus subtilis genome region in the vicinity of the lev
RT   operon reveals two new extracytoplasmic function RNA polymerase sigma
RT   factors SigV and SigZ.";
RL   Microbiology 143:2939-2943(1997).
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the acyltransferase 3 family. {ECO:0000305}.
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DR   EMBL; U93874; AAB80869.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14656.1; -; Genomic_DNA.
DR   PIR; C69975; C69975.
DR   RefSeq; NP_390592.1; NC_000964.3.
DR   RefSeq; WP_004398729.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O05402; -.
DR   SMR; O05402; -.
DR   STRING; 224308.BSU27140; -.
DR   PaxDb; O05402; -.
DR   PRIDE; O05402; -.
DR   EnsemblBacteria; CAB14656; CAB14656; BSU_27140.
DR   GeneID; 936583; -.
DR   KEGG; bsu:BSU27140; -.
DR   PATRIC; fig|224308.179.peg.2947; -.
DR   eggNOG; COG1835; Bacteria.
DR   eggNOG; COG2755; Bacteria.
DR   InParanoid; O05402; -.
DR   OMA; NRWLTNP; -.
DR   PhylomeDB; O05402; -.
DR   BioCyc; BSUB:BSU27140-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0033692; P:cellular polysaccharide biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.40.50.1110; -; 1.
DR   InterPro; IPR002656; Acyl_transf_3_dom.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   Pfam; PF01757; Acyl_transf_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cell membrane; Membrane; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..634
FT                   /note="Putative peptidoglycan O-acetyltransferase YrhL"
FT                   /id="PRO_0000360823"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        244..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        307..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        329..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        385..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          413..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..432
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..474
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   634 AA;  72219 MW;  1FC1AD6A9747020B CRC64;
     MYHKTQHHRY IPGLDGLRAF AVLSVITYHL NFNWANGGFI GVDIFFVLSG YLITSILLPA
     YGNDINLDFR DFWVRRIRRL LPAAYLMIFS TVVWVVLFDR ELLHTVRGDA ISSLFYMSNW
     WFIFHKLSYF DSFGSPSPLK NLWSLAIEEQ FYIIWPMFLV VGMYIMKSRA RLAAVISLLV
     LCSAVMMSVL YEPGGDPSRV YYGTDTRSFE LLIGCALALV WPMKRLSSNR LPSKLKHTLH
     ATEFLAFCIL VLCVYFTDEY EPFLYRGGML FISVTAAILI ACVCHPSSFL GNLLSWRPLR
     WLGTRSYGIY LWHYPVIVLS TPVQEIGNPV FWHIVLKVIV TCILAELSYH FIEKPIRTQG
     FRSFSRRVFI HRIKEWKTTS VISKMSIGFI IFAILIFAGG LSGLAGEQKH PTKWTYSSQE
     TNADTSQASG DKKNAAADKK HNPEQKTTDS NQGQKENKDS GQETHKKKDT QSQQLKKPAD
     TAKEVLAIGD SVMLDISSHL RQSFSNVTID GKVGRQMSQA LELAREYKSF NQPNKAVIIE
     LGTNGYFTNS QIEQLLQSFS KAHIYLVNTR VPRQWESKVN ESLQQQAHAH QNVTLVDWHT
     EALQHPEYFT PDGVHLVPKG AKTLTALIVQ AMKS
 
 
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