(data stored in ACNUC7421 zone)

SWISSPROT: Q3Z4F7_SHISS

ID   Q3Z4F7_SHISS            Unreviewed;       633 AA.
AC   Q3Z4F7;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 74.
DE   RecName: Full=Peptidoglycan D,D-transpeptidase MrdA {ECO:0000256|HAMAP-Rule:MF_02081};
DE            EC=3.4.16.4 {ECO:0000256|HAMAP-Rule:MF_02081};
DE   AltName: Full=Penicillin-binding protein 2 {ECO:0000256|HAMAP-Rule:MF_02081};
DE            Short=PBP-2 {ECO:0000256|HAMAP-Rule:MF_02081};
GN   Name=mrdA {ECO:0000256|HAMAP-Rule:MF_02081,
GN   ECO:0000313|EMBL:AAZ87355.1};
GN   OrderedLocusNames=SSON_0589 {ECO:0000313|EMBL:AAZ87355.1};
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ87355.1, ECO:0000313|Proteomes:UP000002529};
RN   [1] {ECO:0000313|EMBL:AAZ87355.1, ECO:0000313|Proteomes:UP000002529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046 {ECO:0000313|EMBL:AAZ87355.1,
RC   ECO:0000313|Proteomes:UP000002529};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall.
CC       {ECO:0000256|HAMAP-Rule:MF_02081}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also
CC         transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC         substituents of D-alanine.; EC=3.4.16.4;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02081};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02081}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_02081}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_02081}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family. MrdA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02081}.
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; CP000038; AAZ87355.1; -; Genomic_DNA.
DR   EnsemblBacteria; AAZ87355; AAZ87355; SSON_0589.
DR   KEGG; ssn:SSON_0589; -.
DR   HOGENOM; HOG000266120; -.
DR   KO; K05515; -.
DR   OMA; SCDTYYY; -.
DR   BioCyc; SSON300269:G1GL2-692-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002529; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_02081; MrdA_transpept; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR005311; PBP_dimer.
DR   InterPro; IPR036138; PBP_dimer_sf.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   InterPro; IPR017790; Penicillin-binding_protein_2.
DR   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56519; SSF56519; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   TIGRFAMs; TIGR03423; pbp2_mrdA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3Z4F7.
DR   SWISS-2DPAGE; Q3Z4F7.
KW   Carboxypeptidase {ECO:0000256|HAMAP-Rule:MF_02081};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_02081};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02081};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002529};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_02081};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02081};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_02081};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02081}.
FT   TRANSMEM     21     40       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02081}.
FT   DOMAIN       64    239       PBP_dimer. {ECO:0000259|Pfam:PF03717}.
FT   DOMAIN      272    609       Transpeptidase. {ECO:0000259|Pfam:
FT                                PF00905}.
FT   ACT_SITE    330    330       Acyl-ester intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_02081}.
SQ   SEQUENCE   633 AA;  70813 MW;  FCC79506B3B06E67 CRC64;
     MKLQNSFRDY TAESALFVRR ALVAFLGILL LTGVLIANLY NLQIVRFTDY QTRSNENRIK
     LVPIAPSRGI IYDRNGIPLA LNRTIYQIEM MPEKVDNVQQ TLDALRSVVD LTDDDIAAFR
     KERARSHRFT SIPVKTNLTE VQVARFAVNQ YRFPGVEVKG YKRRYYPYGS ALTHVIGYVS
     KINDKDVERL NNDGKLANYA ATHDIGKLGI ERYYEDVLHG QTGYEEVEVN NRGRVIRQLK
     EVPPQAGHDI YLTLDLKLQQ YIETLLAGSR AAVVVTDPRT GGVLALVSTP SYDPNLFVDG
     ISSKDYSALL NAPNTPLVNR ATQGVYPPAS TVKPYVAVSA LSAGVITRNT TLFDPGWWQL
     PGSEKRYRDW KKWGHGRLNV TRSLEESADT FFYQVAYDMG IDRLSEWMGK FGYGHYTGID
     LAEERSGNMP TREWKQKRFK KPWYQGDTIP VGIGQGYWTA TPIQMSKALM ILINDGIVKV
     PHLLMSTAED GKQVPWVQPH EPPVGDIHSG YWELAKDGMY GVANRPNGTA HKYFASAPYK
     IAAKSGTAQV FGLKANETYN AHKIAERLRD HKLMTAFAPY NNPQVAVAMI LENGGAGPAV
     GTLMRQILDH IMLGDNNTDL PAENPAVAAA EDH
//

If you have problems or comments...

PBIL Back to PBIL home page