ID Q4FRE7_PSYA2 Unreviewed; 664 AA.
AC Q4FRE7;
DT 30-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 112.
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=pb {ECO:0000313|EMBL:AAZ19411.1};
GN Synonyms=mrdA {ECO:0000256|HAMAP-Rule:MF_02081};
GN OrderedLocusNames=Psyc_1563 {ECO:0000313|EMBL:AAZ19411.1};
OS Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=259536 {ECO:0000313|EMBL:AAZ19411.1, ECO:0000313|Proteomes:UP000000546};
RN [1] {ECO:0000313|EMBL:AAZ19411.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=273-4 {ECO:0000313|EMBL:AAZ19411.1};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter C., Glavina T.,
RA Hammon N., Israni S., Chain P., Di Bartolo G., Ivanova N., Hauser L.,
RA Land M., Larimer F., Pitluck S., Richardson P.;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAZ19411.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=273-4 {ECO:0000313|EMBL:AAZ19411.1};
RX PubMed=20154119; DOI=10.1128/AEM.02101-09;
RA Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N.,
RA Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C.,
RA Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P.,
RA Murray A., Thomashow M., Tiedje J.M.;
RT "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT Siberian permafrost bacterium, reveals mechanisms for adaptation to low-
RT temperature growth.";
RL Appl. Environ. Microbiol. 76:2304-2312(2010).
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; CP000082; AAZ19411.1; -; Genomic_DNA.
DR RefSeq; WP_011280828.1; NC_007204.1.
DR AlphaFoldDB; Q4FRE7; -.
DR STRING; 259536.Psyc_1563; -.
DR KEGG; par:Psyc_1563; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_1_2_6; -.
DR OrthoDB; 9766847at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000546; 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|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 Glycosyltransferase {ECO:0000313|EMBL:AAZ19411.1};
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:UP000000546};
KW Transferase {ECO:0000313|EMBL:AAZ19411.1};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02081}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
FT DOMAIN 64..233
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 265..600
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT ACT_SITE 324
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
SQ SEQUENCE 664 AA; 73715 MW; 12ECA58DCA335C1E CRC64;
MNKPLTPDTE QVNSIFTSRI LILGLIIFVG LLGLIARYGF LQIFAHDKYT TQSDNNRIKL
ISAPPSRGYI YDRNGIILAD NQPVFTAMLS PDEVGDPERT LQLLAPIFDL TDENITDILA
RLSKNKNDPV TIKIDLTEAQ LAQFSERKPF FRGVTIQSKL TRSYPYDELF AHVIGYVGRI
NDKESKQINK DRYAGTDLIG KIGIEDFYEN ILLGQPGYQS VETDAHGNIL RQLDTKAPIA
GNDITLSLDY GLQVVAQQQL DGRRGAIVAI DPKNGDVLAF VSNPSYDPNP FISGISFKDY
DDLREDLDQP LYNRALQGTY PPGSTIKPFE GLGGIHYGLR NWDTTIYDPG YFSLPGDSHR
FRDWKKGGHG TVDLKQSIVM SVDTYYYKLA YEMGIQRLHD WMVRFGFGEE TGIDLPNEKS
GVMPSPKWKK DTYDKGWLPG ETISVSIGQG YFLATPLQIA NATAMTASKG FHITPHLLKS
SDGAAAVDVI TKPDGKIDYN GKPSDWLRMH DAMEETIKAG TGRGIYTPRY RIAGKTGTAQ
VKSIAQGKSY NKSALDKRQW DHAWFNGFAP VEDPQIALAV LVENGGGGSV VAAPIGRALF
DYWVLQRDTN PILPPTTDQL KVIKRQKAFE KATLDAIRDK EDKALKAAKE KTKAQAQTAT
ATTE
//
