ID Q48HU1_PSE14 Unreviewed; 629 AA.
AC Q48HU1;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 94.
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 OrderedLocusNames=PSPPH_2858 {ECO:0000313|EMBL:AAZ37030.1};
OS Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=264730 {ECO:0000313|EMBL:AAZ37030.1, ECO:0000313|Proteomes:UP000000551};
RN [1] {ECO:0000313|EMBL:AAZ37030.1, ECO:0000313|Proteomes:UP000000551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1448A / Race 6 {ECO:0000313|Proteomes:UP000000551};
RX PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005;
RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA Brinkac L.M., Daugherty S.C., Deboy R., Durkin A.S., Giglio M.G.,
RA Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S., Crabtree J., Creasy T.,
RA Davidsen T., Haft D.H., Zafar N., Zhou L., Halpin R., Holley T., Khouri H.,
RA Feldblyum T., White O., Fraser C.M., Chatterjee A.K., Cartinhour S.,
RA Schneider D.J., Mansfield J., Collmer A., Buell C.R.;
RT "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT 1448A reveals divergence among pathovars in genes involved in virulence and
RT transposition.";
RL J. Bacteriol. 187:6488-6498(2005).
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; CP000058; AAZ37030.1; -; Genomic_DNA.
DR RefSeq; WP_011168829.1; NC_005773.3.
DR AlphaFoldDB; Q48HU1; -.
DR KEGG; psp:PSPPH_2858; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_1_2_6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000551; Chromosome.
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 3: Inferred from homology;
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..41
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
FT DOMAIN 63..234
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 267..603
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT ACT_SITE 326
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
SQ SEQUENCE 629 AA; 70226 MW; 3EC69638A0F4C3FC CRC64;
MPNPIPLKDH EKETRLVNQR LIACAVLVGL LAACLVARMY FLQVTEFDYH STISENNRVH
VLPIPPERGL IFDRNGEVLA DNRPSFNLTL TRERAGDWHK VIDELMTLLE LPDEDRILFD
KELKQVRHPF EPATLLYELT EEQIAILAVN QYLLPGVDVA AQFVRHYPLG AHFAHSIGYV
GRINEKEASH LDNEYRGTQS IGKTGIERFY ESELHGHVGY EEVETNAQGR VLRVLKHTDP
VPGKNITLTL DAHLQAAAEN ALGDRRGSVV ALDPETGEVL AMVSKPSFDP NLFVTGISFK
QYAALRDSID RPLFNRVLRG LYAPGSTVKP EVAIAGLDSG VVTASTKVFD PGYFQLPDFD
HKYRNWNHSG DGWVDMDTAI MRSNDTYFYT VAHKLGIDRL HDYMTMFGIG QKVSLDMFEE
SAGLMPSREW KRATRRQAWF PGETVILGIG QGYMQVTPLQ LAQATSLLAS KGVWHRPHLA
MEVGHDVPLD EHPMPNIVLR DPNEWNQVNT GMQMVMHDPR GIARDAAKGA QYRIAGKSGT
AQVVAIKQGE RYNRLKTLER NRDNALFVGF APADHPKIVV SVTIENGEAG GRVAGPVVRE
ILDAWLLDSE GKLKPQYAVP TKAPGNPHA
//
