ID   Q9X6V3_PSEAI            Unreviewed;       646 AA.
AC   Q9X6V3; A0A1S1BS28; Q7DC85;
DT   01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 157.
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=pbpA {ECO:0000313|EMBL:AAD32230.1};
GN   Synonyms=mrdA {ECO:0000256|HAMAP-Rule:MF_02081,
GN   ECO:0000313|EMBL:MUI36416.1}, penA {ECO:0000313|EMBL:VFT56450.1},
GN   spoVD {ECO:0000313|EMBL:CRQ09200.1};
GN   ORFNames=CAZ10_26315 {ECO:0000313|EMBL:OTI57375.1}, GNQ48_15490
GN   {ECO:0000313|EMBL:MUI36416.1}, GUL26_00100
GN   {ECO:0000313|EMBL:MZZ10634.1}, IPC1295_14660
GN   {ECO:0000313|EMBL:RPM16383.1}, IPC737_17705
GN   {ECO:0000313|EMBL:RPW72048.1}, NCTC13621_06836
GN   {ECO:0000313|EMBL:VFT56450.1}, PA52Ts2_5394
GN   {ECO:0000313|EMBL:QJE86795.1}, PAERUG_P19_London_7_VIM_2_05_10_06701
GN   {ECO:0000313|EMBL:CRQ09200.1};
OS   Pseudomonas aeruginosa.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287 {ECO:0000313|EMBL:AAD32230.1};
RN   [1] {ECO:0000313|EMBL:AAD32230.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PAO1 {ECO:0000313|EMBL:AAD32230.1};
RA   Gagnon L.A., Castro-Urbina I.M., Liao X., Hancock R.E.W., Clarke A.J.,
RA   Huletsky A.;
RT   "Cloning and characterization of PBP5 of Pseudomonas aeruginosa.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000045039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P19_London_7_VIM_2_05_10 {ECO:0000313|Proteomes:UP000045039};
RA   Radhakrishnan Rajesh, Underwood Anthony, Al-Shahib Ali;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:CRQ09200.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=P19_London_7_VIM_2_05_10 {ECO:0000313|EMBL:CRQ09200.1};
RA   Radhakrishnan R., Underwood A., Al-Shahib A.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:OTI57375.1, ECO:0000313|Proteomes:UP000194857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S567_C10_BS {ECO:0000313|EMBL:OTI57375.1,
RC   ECO:0000313|Proteomes:UP000194857};
RA   Song R., Chenine A.L., Ruprecht R.M.;
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|Proteomes:UP000284767, ECO:0000313|Proteomes:UP000284878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CPHL10662 {ECO:0000313|EMBL:RPW72048.1,
RC   ECO:0000313|Proteomes:UP000284878}, and PA-W36
RC   {ECO:0000313|EMBL:RPM16383.1, ECO:0000313|Proteomes:UP000284767};
RA   Feschi L., Jeukens J., Emond-Rheault J.-G., Kukavica-Ibrulj I., Boyle B.,
RA   Levesque R.C.;
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|Proteomes:UP000284767, ECO:0000313|Proteomes:UP000284878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CPHL10662 {ECO:0000313|EMBL:RPW72048.1,
RC   ECO:0000313|Proteomes:UP000284878}, and PA-W36
RC   {ECO:0000313|EMBL:RPM16383.1, ECO:0000313|Proteomes:UP000284767};
RA   Freschi L., Vincent A.T., Jeukens J., Emond-Rheault J.-G.,
RA   Kukavica-Ibrulj I., Dupont M.-J., Charette S.J., Boyle B., Levesque R.C.;
RT   "The Pseudomonas aeruginosa pan-genome provides new insights on its
RT   population structure, horizontal gene transfer and pathogenicity.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:VFT56450.1, ECO:0000313|Proteomes:UP000344659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC13621 {ECO:0000313|EMBL:VFT56450.1,
RC   ECO:0000313|Proteomes:UP000344659};
RG   Pathogen Informatics;
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
RN   [8] {ECO:0000313|EMBL:MUI36416.1, ECO:0000313|Proteomes:UP000433532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA221 {ECO:0000313|EMBL:MUI36416.1,
RC   ECO:0000313|Proteomes:UP000433532};
RA   Khan M., Rice S.A., Willcox M.D.P., Stapleton F.;
RT   "Genomes of ocular Pseudomonas aeruginosa isolates.";
RL   Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
RN   [9] {ECO:0000313|EMBL:MZZ10634.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VNMU148 {ECO:0000313|EMBL:MZZ10634.1};
RA   Snesrud E., Galac M.R., Mc Gann P., Valentine K., Viacheslav K.;
RT   "Bacteria Cultured from War Wounds Associated with the Conflict in Eastern
RT   Ukraine.";
RL   Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
RN   [10] {ECO:0000313|EMBL:QJE86795.1, ECO:0000313|Proteomes:UP000502341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GIMC5020:PA52Ts2 {ECO:0000313|EMBL:QJE86795.1,
RC   ECO:0000313|Proteomes:UP000502341};
RA   Voronina O.L., Kunda M.S., Aksenova E.I., Ryzhova N.N., Semenov A.N.;
RL   Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
RN   [11] {ECO:0007829|PDB:7KIS}
RP   X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS).
RX   PubMed=33593978; DOI=10.1128/mbio.03058-20;
RA   Rajavel M., Kumar V., Nguyen H., Wyatt J., Marshall S.H.,
RA   Papp-Wallace K.M., Deshpande P., Bhavsar S., Yeole R., Bhagwat S.,
RA   Patel M., Bonomo R.A., van den Akker F.;
RT   "Structural Characterization of Diazabicyclooctane beta-Lactam "Enhancers"
RT   in Complex with Penicillin-Binding Proteins PBP2 and PBP3 of Pseudomonas
RT   aeruginosa. .";
RL   MBio 12:e03058-e03020(2021).
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; Evidence={ECO:0000256|HAMAP-
CC         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}. Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family. MrdA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02081}.
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DR   EMBL; AF147448; AAD32230.1; -; Genomic_DNA.
DR   EMBL; CVVU01000271; CRQ09200.1; -; Genomic_DNA.
DR   EMBL; WOAD01000011; MUI36416.1; -; Genomic_DNA.
DR   EMBL; WXZT01000001; MZZ10634.1; -; Genomic_DNA.
DR   EMBL; NFFZ01000017; OTI57375.1; -; Genomic_DNA.
DR   EMBL; CP051768; QJE86795.1; -; Genomic_DNA.
DR   EMBL; NSNE01000007; RPM16383.1; -; Genomic_DNA.
DR   EMBL; NSTV01000006; RPW72048.1; -; Genomic_DNA.
DR   EMBL; CAADJP010000012; VFT56450.1; -; Genomic_DNA.
DR   PIR; G83146; G83146.
DR   RefSeq; NP_252692.1; NC_002516.2.
DR   RefSeq; WP_003093191.1; NZ_WYAF01000020.1.
DR   PDB; 7KIS; X-ray; 2.87 A; A/B=1-646.
DR   ChEMBL; CHEMBL5539; -.
DR   DrugBank; DB01413; Cefepime.
DR   DrugBank; DB14879; Cefiderocol.
DR   GeneID; 878962; -.
DR   KEGG; pae:PA4003; -.
DR   PATRIC; fig|287.1477.peg.1343; -.
DR   OMA; GMYEVCN; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000045039; Unassembled WGS sequence.
DR   Proteomes; UP000194857; Unassembled WGS sequence.
DR   Proteomes; UP000284767; Unassembled WGS sequence.
DR   Proteomes; UP000284878; Unassembled WGS sequence.
DR   Proteomes; UP000344659; Unassembled WGS sequence.
DR   Proteomes; UP000433532; Unassembled WGS sequence.
DR   Proteomes; UP000502341; Chromosome.
DR   Proteomes; UP000644192; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:7KIS};
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645, ECO:0000256|HAMAP-
KW   Rule:MF_02081}; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_02081};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, 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
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
FT   DOMAIN          63..235
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          268..604
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   ACT_SITE        327
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
SQ   SEQUENCE   646 AA;  72213 MW;  2F4CA6F5746CCCB1 CRC64;
     MPQPIHLKDH EKDARLVRRR VIVGAVAVVL LTLVLVARMY HLQVTQYEYH STLSENNRVH
     VQPIPPTRGI IFDRNGVIIA DNRPSFSLTI TRERTEDLQK TLDTLVEILG LTEDDRAIFE
     KRMKQGRRPF EPVPIMFELN EEQIARIAVN QFRLPGVDVA TQFVRHYPLK EHFAHSVGYV
     GRINEQELKN LDPINYSGTH HIGKTGIERF YESELHGTVG YEEVETNARG RVLRVLKRTD
     PIPGKDIVLS IDSRLQEAAE NALAGRRGAI VAIQPSTGDV LAMVSQPSYD PNLFVTGISF
     KAYAELRDSI DRPLYNRVLR GLYPPGSTVK PAVALAGLDA GVVTPTSRVF DPGYYQLPNY
     DHKYRNWNRY GDGWVSLESA IYRSNDTYFY DLAHKLGIDR LHAFMSRFGF GQKVALDMFG
     EADGLMPSRE WKRKTRRQVW YPGETLILGI GQGYMQATPI QLAQMTALLA NKGHWIRPHL
     AKTIDGQPPV DPDPMPDIVL RDPANWDRVD YGMQQVVHGA RGTARKVGAT SAYLIAGKSG
     TAQVVAIKQN ERYDRSKLLE RHRDHALFVG FAPANNPQIA VAVMVENGES GSGVAAPVVK
     QVMDAWLLDE HGKLKAEYAE PVAPLAAAVA KPEPTAAEPE APALEQ
//