位置:首页 > 蛋白库 > MLTC_YERPE
MLTC_YERPE
ID   MLTC_YERPE              Reviewed;         358 AA.
AC   Q8ZHE6; Q0WI88; Q74QI2; Q7CGR3;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   25-MAY-2022, entry version 134.
DE   RecName: Full=Membrane-bound lytic murein transglycosylase C {ECO:0000255|HAMAP-Rule:MF_01616};
DE            EC=4.2.2.n1 {ECO:0000255|HAMAP-Rule:MF_01616};
DE   AltName: Full=Murein lyase C {ECO:0000255|HAMAP-Rule:MF_01616};
DE   Flags: Precursor;
GN   Name=mltC {ECO:0000255|HAMAP-Rule:MF_01616};
GN   OrderedLocusNames=YPO0954, y3341, YP_3487;
OS   Yersinia pestis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO-92 / Biovar Orientalis;
RX   PubMed=11586360; DOI=10.1038/35097083;
RA   Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA   Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA   Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA   Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA   Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA   Stevens K., Whitehead S., Barrell B.G.;
RT   "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL   Nature 413:523-527(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIM10+ / Biovar Mediaevalis;
RX   PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA   Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA   Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA   Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA   Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT   "Genome sequence of Yersinia pestis KIM.";
RL   J. Bacteriol. 184:4601-4611(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91001 / Biovar Mediaevalis;
RX   PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA   Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA   Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA   Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA   Wang J., Huang P., Yang R.;
RT   "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT   avirulent to humans.";
RL   DNA Res. 11:179-197(2004).
CC   -!- FUNCTION: Murein-degrading enzyme. May play a role in recycling of
CC       muropeptides during cell elongation and/or cell division.
CC       {ECO:0000255|HAMAP-Rule:MF_01616}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exolytic cleavage of the (1->4)-beta-glycosidic linkage
CC         between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine
CC         (GlcNAc) residues in peptidoglycan, from either the reducing or the
CC         non-reducing ends of the peptidoglycan chains, with concomitant
CC         formation of a 1,6-anhydrobond in the MurNAc residue.; EC=4.2.2.n1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01616};
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01616}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_01616}.
CC   -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC       {ECO:0000255|HAMAP-Rule:MF_01616}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM86891.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAS63642.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAL19620.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL590842; CAL19620.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE009952; AAM86891.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE017042; AAS63642.1; ALT_INIT; Genomic_DNA.
DR   PIR; AB0117; AB0117.
DR   RefSeq; WP_002209995.1; NZ_WUCM01000030.1.
DR   AlphaFoldDB; Q8ZHE6; -.
DR   SMR; Q8ZHE6; -.
DR   IntAct; Q8ZHE6; 1.
DR   STRING; 214092.YPO0954; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   PaxDb; Q8ZHE6; -.
DR   EnsemblBacteria; AAM86891; AAM86891; y3341.
DR   EnsemblBacteria; AAS63642; AAS63642; YP_3487.
DR   GeneID; 66844343; -.
DR   KEGG; ype:YPO0954; -.
DR   KEGG; ypk:y3341; -.
DR   KEGG; ypm:YP_3487; -.
DR   eggNOG; COG0741; Bacteria.
DR   HOGENOM; CLU_044583_0_0_6; -.
DR   OMA; AIMQIES; -.
DR   Proteomes; UP000000815; Chromosome.
DR   Proteomes; UP000001019; Chromosome.
DR   Proteomes; UP000002490; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008933; F:lytic transglycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR   HAMAP; MF_01616; MltC; 1.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR023664; Murein_transglycosylaseC.
DR   InterPro; IPR024570; Murein_transglycosylaseC_N.
DR   InterPro; IPR000189; Transglyc_AS.
DR   InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR   Pfam; PF11873; Mltc_N; 1.
DR   Pfam; PF01464; SLT; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Cell wall biogenesis/degradation; Lipoprotein; Lyase;
KW   Membrane; Palmitate; Reference proteome; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01616"
FT   CHAIN           17..358
FT                   /note="Membrane-bound lytic murein transglycosylase C"
FT                   /id="PRO_0000032799"
FT   LIPID           17
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01616"
FT   LIPID           17
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01616"
SQ   SEQUENCE   358 AA;  39947 MW;  DA79BBFD6951C952 CRC64;
     MKKILALLVI APLLVSCSGN KNQVENEVFV KDTNGFEILM GQFAHNIENI WGLKEVLIAG
     PKDYVKYTDQ YQTRSHINFD AGTITIETIA TTNPAAHLRQ AIITTLLMGD DPGSIDLYSD
     VNDIQISKEP FLYGQVLDNN GEPIRWEWRA AHFADYLLQN KMQTRTSGLH VISFVTIQLV
     PNHLDKRAHK YLPLVRKSAA RYGVEESLIL AIMQTESSFN PYAVSRSDAL GLMQVVQHTA
     GKDVFKLKGK SGQPSRSYLF DPENNIDAGT AYLSILQNTY LGGIQNATSR RYAVITSYNG
     GAGSVLRVFH SDKNKAVGII NTMSPGDVFQ TLTTKHPSGE SRRYLVKVNS AQKNYRRY
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025