ID A0A2I6SA90_9RHOO Unreviewed; 632 AA.
AC A0A2I6SA90;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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:AUN96173.1};
GN ORFNames=C0099_15235 {ECO:0000313|EMBL:AUN96173.1};
OS Pseudazoarcus pumilus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Pseudazoarcus.
OX NCBI_TaxID=2067960 {ECO:0000313|EMBL:AUN96173.1, ECO:0000313|Proteomes:UP000242205};
RN [1] {ECO:0000313|EMBL:AUN96173.1, ECO:0000313|Proteomes:UP000242205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY39 {ECO:0000313|EMBL:AUN96173.1,
RC ECO:0000313|Proteomes:UP000242205};
RA Fu G.-Y.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass 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; CP025682; AUN96173.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I6SA90; -.
DR KEGG; atw:C0099_15235; -.
DR OrthoDB; 9789078at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000242205; Chromosome.
DR GO; GO:0005886; C: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; 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 {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 Hydrolase {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 Reference proteome {ECO:0000313|Proteomes:UP000242205};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02081}.
FT DOMAIN 61..234
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 268..606
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 632 AA; 69908 MW; 4035824094865254 CRC64;
MTEFRAPQEA LFRFRRRAVV AAVFVALCFV VLAARLYHLQ VAQYDYFHSR AEGNRVAVLP
VVPRRGVIHD RHGEVLARNY SAWTVEINPA QVRDLDAALA ELGEVLPFDE RDDRRFRRRL
QETKYFESVP LRTHLNDEEV AAVAARLYRL PGVELRARLF RDYPNGESAA HAIGYIGRIN
ERELQRIDAR GETANYRGSE YMGKSGIELA YERELHGVTG VEQIEVNASG RAVRLLARTA
PVNGSDLELS LHMGLQRAAE AALGSRRGAV VAIEPATGEV LALVSTPSYD PNLFIDGISV
ADWRALSDSP EHPLLNRAIY SAYPPGSTYK PFMALAGLAS GIRMPEDSFD NQGLFTVGAQ
RLVDRKSKCQ HGVDLHRSIV YSCNTYYYEL AHEMGIEAIA AFMSQFGFGS RTGIDIPGEA
PGVLPSPAWK RARFKSREHQ QWYGGETISV AIGQGYNAYT PLQMAHALSV VLNYGEVRRP
HLVRRIVDGL SGEIRHPASQ PERFVPLVRS HVDALKRAMV DVTKVGTASA VFADAPYDAG
GKTGTAQVFS LRGQKYVSEE LAERLRDHAW FIGFAPAEAP TIALAVFVEN GGFGSQSAAP
VARKLFDYYL LGRRVESQAG ELDEVVATEL EP
//
