ID   MRDA_HAEIN              Reviewed;         651 AA.
AC   P44469;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 135.
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=pbp2;
GN   OrderedLocusNames=HI_0032;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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   -!- DOMAIN: Has a penicillin insensitive transglycosylase domain (formation
CC       of linear glycan strands) and a penicillin-sensitive transpeptidase
CC       domain (cross-linking of the peptide subunits).
CC   -!- SIMILARITY: Belongs to the transpeptidase family. MrdA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_02081}.
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DR   EMBL; L42023; AAC21710.1; -; Genomic_DNA.
DR   PIR; C64044; C64044.
DR   RefSeq; NP_438205.1; NC_000907.1.
DR   AlphaFoldDB; P44469; -.
DR   SMR; P44469; -.
DR   STRING; 71421.HI_0032; -.
DR   DrugBank; DB00671; Cefixime.
DR   DrugBank; DB00303; Ertapenem.
DR   EnsemblBacteria; AAC21710; AAC21710; HI_0032.
DR   KEGG; hin:HI_0032; -.
DR   PATRIC; fig|71421.8.peg.32; -.
DR   eggNOG; COG0768; Bacteria.
DR   HOGENOM; CLU_009289_1_2_6; -.
DR   OrthoDB; 9766847at2; -.
DR   PhylomeDB; P44469; -.
DR   BioCyc; HINF71421:G1GJ1-32-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008658; F:penicillin binding; IBA:GO_Central.
DR   GO; GO:0071972; F:peptidoglycan L,D-transpeptidase activity; IBA:GO_Central.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
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; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 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   NCBIfam; TIGR03423; pbp2_mrdA; 1.
DR   PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30627:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 1.
DR   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 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; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..651
FT                   /note="Peptidoglycan D,D-transpeptidase MrdA"
FT                   /id="PRO_0000195448"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02081"
FT   ACT_SITE        338
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02081"
SQ   SEQUENCE   651 AA;  73813 MW;  4BEB73290952AAB0 CRC64;
     MNLKKFFNTP THEPFRDKKA ERNLFARRTL VAFLGILLLT GVLFTNIYQL QIVNFDTYQT
     RSNGNRIKLL PLPPTRGLIY DRYGKLLAEN LTFFGLYIVP EKTENLDRTL DELRYIVGLT
     DNDIENFKKE RRRGTRYTPI LLKPNLTEEQ ISRFAVNGYQ YPSLEVRPYF KRHYLYGETM
     AHILGYVGKM NDKDVERLKR EDKFANYAGT NDIGKLGIER YYEDILQGTT GFEEVEINNR
     GKVIRTLRSR PAVAGKSIHL TIDLALQRYI TELLSGLKGA VVVLDPKDSS VLAMVSTPSY
     DNNLFVDGIS SEDYKRLLND LARPLYSRAT QGAYPPASTV KPFIAVAAQT ENVITPNTTI
     FDPGYWVLPN STKRFRDWKK TGHGDTDLNK AITESSDTYF YQVAYNMGID RLSNWMKDFG
     FGMPTGIEIQ EETAANIPTR EWKQKRYKRP WVQGDTISVG IGQGYWTATP LQVAKATTIL
     VNNGKVNTPH LMKAIEGAVL EPYEDPLLYP DINTPKVAAW EAAKRGMYNV VNAANGTGRK
     AFADANYRVA GKSGTAQVFS LKENEKYNTA GLKKELHDHA WFTAYAPYDN PKLVVTVILE
     NAGGGSSNAA PLARKVMDYY LNQRLPQVEK YNVPIQQKKD LSQESEQING R
//