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RLPA_HELPY
ID   RLPA_HELPY              Reviewed;         315 AA.
AC   O26091;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=Endolytic peptidoglycan transglycosylase RlpA {ECO:0000255|HAMAP-Rule:MF_02071};
DE            EC=4.2.2.- {ECO:0000255|HAMAP-Rule:MF_02071};
DE   Flags: Precursor;
GN   Name=rlpA {ECO:0000255|HAMAP-Rule:MF_02071}; OrderedLocusNames=HP_1571;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
CC   -!- FUNCTION: Lytic transglycosylase with a strong preference for naked
CC       glycan strands that lack stem peptides. {ECO:0000255|HAMAP-
CC       Rule:MF_02071}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_02071};
CC       Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_02071}.
CC   -!- SIMILARITY: Belongs to the RlpA family. {ECO:0000255|HAMAP-
CC       Rule:MF_02071}.
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DR   EMBL; AE000511; AAD08608.1; -; Genomic_DNA.
DR   PIR; C64716; C64716.
DR   RefSeq; NP_208362.1; NC_000915.1.
DR   RefSeq; WP_000521815.1; NC_018939.1.
DR   AlphaFoldDB; O26091; -.
DR   SMR; O26091; -.
DR   DIP; DIP-3473N; -.
DR   IntAct; O26091; 1.
DR   MINT; O26091; -.
DR   STRING; 85962.C694_08140; -.
DR   PaxDb; O26091; -.
DR   EnsemblBacteria; AAD08608; AAD08608; HP_1571.
DR   KEGG; hpy:HP_1571; -.
DR   PATRIC; fig|85962.47.peg.1689; -.
DR   eggNOG; COG0797; Bacteria.
DR   OMA; MGAFRNQ; -.
DR   PhylomeDB; O26091; -.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008932; F:lytic endotransglycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000270; P:peptidoglycan metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.40.10; -; 1.
DR   Gene3D; 3.30.70.1070; -; 1.
DR   HAMAP; MF_02071; RlpA; 1.
DR   InterPro; IPR034718; RlpA.
DR   InterPro; IPR009009; RlpA-like_DPBB.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   InterPro; IPR012997; RplA.
DR   InterPro; IPR007730; SPOR-like_dom.
DR   InterPro; IPR036680; SPOR-like_sf.
DR   Pfam; PF03330; DPBB_1; 1.
DR   Pfam; PF05036; SPOR; 1.
DR   SUPFAM; SSF110997; SSF110997; 1.
DR   SUPFAM; SSF50685; SSF50685; 1.
DR   TIGRFAMs; TIGR00413; rlpA; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS51724; SPOR; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cell wall biogenesis/degradation; Lipoprotein; Lyase;
KW   Membrane; Palmitate; Reference proteome; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT   CHAIN           20..315
FT                   /note="Endolytic peptidoglycan transglycosylase RlpA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT                   /id="PRO_0000030804"
FT   DOMAIN          242..315
FT                   /note="SPOR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT   REGION          68..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           20
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT   LIPID           20
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
SQ   SEQUENCE   315 AA;  35476 MW;  194402D94C1FC14D CRC64;
     MGLALEKVCF LGVIFLISAC TVKKEGVKNL SYKHESLRAY ENAKDYDPTT KKAAYKRNFF
     ERHFKRYSDS QDSNTKDQPL DNGMRDSSSI QRATMRPYQV GGKWYYPTKV DLGEKFDGVA
     SWYGPNFHAK KTSNGEIYNM YAHTAAHKTL PMNTVVKVIN VDNNLSTIVR INDRGPFVSD
     RIIDLSNAAA RDIDMVKKGT ASVRLIVLGF GGVISTQYEQ SFNASSSKIL HKEFKVGESE
     KSVSGGKFSL QMGAFRNQIG AQTLADKLQA ENPNYSVKVA FKDDLYKVLV QGFQSEEEAR
     DFMKKYNQNA VLTRE
 
 
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