ID A0A2N7VLH7_9BURK Unreviewed; 812 AA.
AC A0A2N7VLH7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:PMS17999.1};
GN ORFNames=C0Z19_23600 {ECO:0000313|EMBL:PMS17999.1};
OS Trinickia soli.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Trinickia.
OX NCBI_TaxID=380675 {ECO:0000313|EMBL:PMS17999.1, ECO:0000313|Proteomes:UP000235347};
RN [1] {ECO:0000313|EMBL:PMS17999.1, ECO:0000313|Proteomes:UP000235347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GP25-8 {ECO:0000313|EMBL:PMS17999.1,
RC ECO:0000313|Proteomes:UP000235347};
RA Estrada-de los Santos P., Palmer M., Chavez-Ramirez B., Beukes C.,
RA Steenkamp E.T., Hirsch A.M., Manyaka P., Maluk M., Lafos M., Crook M.,
RA Gross E., Simon M.F., Bueno dos Reis Junior F., Poole P.S., Venter S.N.,
RA James E.K.;
RT "Whole genome analyses suggest that Burkholderia sensu lato contains two
RT further novel genera in the rhizoxinica-symbiotica group Mycetohabitans
RT gen. nov., and Trinickia gen. nov.: implications for the evolution of
RT diazotrophy and nodulation in the Burkholderiaceae.";
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: 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PMS17999.1}.
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DR EMBL; PNYB01000027; PMS17999.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N7VLH7; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000235347; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000235347};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02081}.
FT TRANSMEM 21..42
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
FT DOMAIN 61..251
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 283..623
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 185..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..792
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 342
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
SQ SEQUENCE 812 AA; 87247 MW; 219380A6755C6D03 CRC64;
MTEFKNTQQQ LMRFRFRVAA AGLFVLACFG LLVLRFLFLQ VWHYSKYSLQ ADENRISVAP
IVPNRGIITD RNGVVLARNY SAYTLEITPS KLDDTLDHVI DKLATVITID ARDRHRFKKL
LEDSKNFESL PIRTRLTDEE VARFTAQRFR FPGVDVRARL FRQYPLGTTA AHVIGYIGRI
SQRDQEKIDA VSEQNDSDPD HYDPRLDANN YKGTDYIGKI GVEQSYEAEL HGLTGFEEVE
VTAGGRPVRT LSRTQATPGN NLVLSLDIGV QEVAEQAFAG HRGALVAIEP STGDVLAFVS
APSFDPNAFV DGIDQQTWDE LNNSPDHPLL NRPLHSAYPP GSTYKPFMAL AALTLHKRTP
EWGFHDPGFY QFGGHTFRND VPQGQGWIDM NRAIMVSNDT YFYMLAHDLG VNTIADFMKP
WGFGQITGID ISGEARGILP STEWKKKAYR KPEQQRWYEG ETISLGIGQG YNSFTMLQLA
HATATLANDG IVMRPHLVKE IENPITHDMR LTVPHESGRI AVSQADIDVV KRGMVAVTSN
PSGTGYEVFR NAPYTVAGKT GTAQVFSLQG AKYHGGALAE HLRDHSLFIA FAPADHPVIA
VATIVENGGW GASVAGPIVR RVLDYYLLQR GKPGVLQAEV AAAASATQGI PGPVIGASEP
ADAAGAAEGA TAPVKVAAGF KALPLPALPA SAPREVSAPL IASDVVAAQR AAASGSSASA
AAAAQSPGSA QAGAAASRSS ASAPPASAAE VIRRLHRAAA SSAATNDAAG SPPKRHPSRR
EPASDALVAP REDRTDAQPP AATTPGAPGP ND
//
