MRDA_HAEIN
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 03-AUG-2022, entry version 128.
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; Proteobacteria; 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 RefSeq; WP_005649850.1; NC_000907.1.
DR AlphaFoldDB; P44469; -.
DR SMR; P44469; -.
DR STRING; 71421.HI_0032; -.
DR DrugBank; DB00671; Cefixime.
DR DrugBank; DB00303; Ertapenem.
DR PRIDE; P44469; -.
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 OMA; SCDTYYY; -.
DR PhylomeDB; P44469; -.
DR BioCyc; HINF71421:G1GJ1-32-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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; -; 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; 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
