ID I0HYB0_RUBGI Unreviewed; 708 AA.
AC I0HYB0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
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:BAL97997.1};
GN OrderedLocusNames=RGE_46640 {ECO:0000313|EMBL:BAL97997.1};
OS Rubrivivax gelatinosus (strain NBRC 100245 / IL144).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Rubrivivax.
OX NCBI_TaxID=983917 {ECO:0000313|EMBL:BAL97997.1, ECO:0000313|Proteomes:UP000007883};
RN [1] {ECO:0000313|EMBL:BAL97997.1, ECO:0000313|Proteomes:UP000007883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100245 / IL144 {ECO:0000313|Proteomes:UP000007883};
RX PubMed=22689232; DOI=10.1128/JB.00511-12;
RA Nagashima S., Kamimura A., Shimizu T., Nakamura-isaki S., Aono E.,
RA Sakamoto K., Ichikawa N., Nakazawa H., Sekine M., Yamazaki S., Fujita N.,
RA Shimada K., Hanada S., Nagashima K.V.P.;
RT "Complete genome sequence of phototrophic betaproteobacterium Rubrivivax
RT gelatinosus IL144.";
RL J. Bacteriol. 194:3541-3542(2012).
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; AP012320; BAL97997.1; -; Genomic_DNA.
DR AlphaFoldDB; I0HYB0; -.
DR STRING; 983917.RGE_46640; -.
DR KEGG; rge:RGE_46640; -.
DR PATRIC; fig|983917.3.peg.4546; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_1_2_4; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000007883; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
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 Glycosyltransferase {ECO:0000313|EMBL:BAL97997.1};
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:UP000007883};
KW Transferase {ECO:0000313|EMBL:BAL97997.1};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02081}.
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
FT DOMAIN 61..239
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 272..611
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 626..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..693
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 331
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
SQ SEQUENCE 708 AA; 77359 MW; 74038D1EB2E6737D CRC64;
MTEIKDLELE LGRFRARLFA AAAFVLVAFG LLTTRLVYLQ VVRHDELATQ AENNRIAIVP
IVPNRGLIVD RNGVVLATNY SAYTLEITPS RIGDVDLDEL IDQLGRYVEI QPRDRRRFKR
QMEESKGFDS LPIRTKLSDE EVARFIAQRF RFPGVDVKAR LFRQYPLGEV GSHLLGYIGR
INQAEKKAMS DWPEEQQDNY RGTEYIGKLG LEQSYEQELH GTTGFEEVET SANGRAVRRL
DSHPPTPGNK LVLSIDIKLQ ALVEQMFGDR RGALVAIDPR NGEILAFVSK PTFDPNLFVD
GIDVESWKEL NESIDRPLLN RALRGTYPPG STYKPFMAIN ALQSGKRSAS LVIQDNASWT
FGNHTFRSHG DIALGPVDMH RAIVKSSNVY FYSLANDMGV DLIHDMMAPF GFGQRTGIDL
EGEVTGVLPS TEWKRKTYKR PEQQRWYAGE TISLGIGQGY NNFTMLQMAN AMATLASGGQ
RYTPHLVREV EDVITRERRQ VAAKPREPLP LKPENVAVVM RALQGVVQEG TGAGAFAGAP
YTSGGKTGTA QAVTIRSNEK YNAAKLEEHK RDHALYTALA PMEAPRVALA VIVENAGFGA
ASAAPIARRV IDYLLLGQYP SEEDLAALRG GRSGPPIGTP RRAADVPLPG QTPAAVDAAA
SAASAAATLA AAPPAPAPSA PPRRDPAPVP ALAPPAGAAS DVQKVARR
//
