ID   MRDA_SALTS              Reviewed;         623 AA.
AC   E1WGF1; P74872;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Peptidoglycan D,D-transpeptidase MrdA {ECO:0000255|HAMAP-Rule:MF_02081};
DE            EC=3.4.16.4 {ECO:0000255|HAMAP-Rule:MF_02081};
DE   AltName: Full=Penicillin-binding protein 2 {ECO:0000255|HAMAP-Rule:MF_02081};
DE            Short=PBP-2 {ECO:0000255|HAMAP-Rule:MF_02081};
GN   Name=mrdA {ECO:0000255|HAMAP-Rule:MF_02081}; Synonyms=pbpA;
GN   OrderedLocusNames=SL1344_1845;
OS   Salmonella typhimurium (strain SL1344).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=216597;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL1344;
RX   PubMed=22538806; DOI=10.1073/pnas.1201061109;
RA   Kroger C., Dillon S.C., Cameron A.D., Papenfort K., Sivasankaran S.K.,
RA   Hokamp K., Chao Y., Sittka A., Hebrard M., Handler K., Colgan A.,
RA   Leekitcharoenphon P., Langridge G.C., Lohan A.J., Loftus B., Lucchini S.,
RA   Ussery D.W., Dorman C.J., Thomson N.R., Vogel J., Hinton J.C.;
RT   "The transcriptional landscape and small RNAs of Salmonella enterica
RT   serovar Typhimurium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:E1277-E1286(2012).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-106.
RC   STRAIN=SL1344;
RX   PubMed=8930920; DOI=10.1046/j.1365-2958.1996.00120.x;
RA   Valdivia R.H., Falkow S.;
RT   "Bacterial genetics by flow cytometry: rapid isolation of Salmonella
RT   typhimurium acid-inducible promoters by differential fluorescence
RT   induction.";
RL   Mol. Microbiol. 22:367-378(1996).
CC   -!- FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall.
CC       {ECO:0000255|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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02081};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02081}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_02081}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_02081}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family. MrdA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_02081}.
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DR   EMBL; FQ312003; CBW17939.1; -; Genomic_DNA.
DR   EMBL; U62714; AAC44611.1; -; Genomic_DNA.
DR   RefSeq; WP_000142877.1; NZ_QASL01000015.1.
DR   AlphaFoldDB; E1WGF1; -.
DR   SMR; E1WGF1; -.
DR   EnsemblBacteria; CBW17939; CBW17939; SL1344_1845.
DR   KEGG; sey:SL1344_1845; -.
DR   PATRIC; fig|216597.6.peg.2048; -.
DR   HOGENOM; CLU_009289_1_2_6; -.
DR   OMA; TLACKTG; -.
DR   BioCyc; SENT216597:SL1344_RS09555-MON; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000008962; 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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; -; 1.
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;
KW   Carboxypeptidase; Cell inner membrane; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Hydrolase; Membrane;
KW   Peptidoglycan synthesis; Protease; Transmembrane; Transmembrane helix.
FT   CHAIN           1..623
FT                   /note="Peptidoglycan D,D-transpeptidase MrdA"
FT                   /id="PRO_0000405425"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02081"
FT   ACT_SITE        326
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02081"
FT   CONFLICT        62
FT                   /note="P -> A (in Ref. 2; AAC44611)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        103
FT                   /note="P -> R (in Ref. 2; AAC44611)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   623 AA;  69833 MW;  F59E950C293A5E71 CRC64;
     MTFKDFDAEE KLFLRRVIVA FGVVVVCFGI LIFNLYNLQI RQHHYYTTRS NENDIKMLPV
     APTRGIIYDR NGIPLVRNVT WYDIAVTPYK IADMDALLKQ LTPIVDLSPD DISDFRRALK
     SSSRYRPVVL KNALTDVEIA RFAVNQFHFN GVTINSYQDR QYPYGAELAH VLGYVSKIND
     NDLKALDKKG LAENYAADHN IGKQGIERYY ENDLHGKTGY QEVEVDNHGR IVRLLKDVPP
     IAGKNIHLTL DLHLQEYIES LLAGQRAAVL VEDPHDGSVL AMVSMPSYDP NPFVKGISYQ
     DYGKLLHDKN LPLINRVTQG LYPPASTVKP YMAMSALLCG IITPQTTFFG APTWTLPGTQ
     RHYRDWKKTG HGMLDVTKAI EESADTFFYQ VAYMMGIDRI DTMLSQFGYG KPTGIDLNEE
     YDGLLPSRAW KQRVHKKAWY QGDTISVGIG QGYWIATPIQ MVKAMVALIN NGKVIAPHLL
     LNEESGKTVV PYRPSGTPAQ IADPASPYWG LVRQAMYGMA NAPNGTGYKF FHTAPYGIAA
     KSGTSQVFSL KENQTYNAKM IPIRLRDHVF YTAFAPYKNP KVAIALILEN GGSDGVTAAP
     IMRKILDHLF DPQADTTQPD QAP