ID F6D994_THICA Unreviewed; 599 AA.
AC F6D994;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=Thicy_1254 {ECO:0000313|EMBL:AEG32021.1};
OS Thiomicrospira cyclica (strain DSM 14477 / JCM 11371 / ALM1)
OS (Thioalkalimicrobium cyclicum).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Thiomicrospira.
OX NCBI_TaxID=717773 {ECO:0000313|EMBL:AEG32021.1, ECO:0000313|Proteomes:UP000009232};
RN [1] {ECO:0000313|EMBL:AEG32021.1, ECO:0000313|Proteomes:UP000009232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14477 / JCM 11371 / ALM1
RC {ECO:0000313|Proteomes:UP000009232};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Davenport K., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Kappler U., Woyke T.;
RT "Complete sequence of Thioalkalimicrobium cyclicum ALM1.";
RL Submitted (MAY-2011) 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; CP002776; AEG32021.1; -; Genomic_DNA.
DR AlphaFoldDB; F6D994; -.
DR STRING; 717773.Thicy_1254; -.
DR KEGG; tcy:Thicy_1254; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_1_2_6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000009232; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
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:AEG32021.1};
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:UP000009232};
KW Transferase {ECO:0000313|EMBL:AEG32021.1};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02081}.
FT DOMAIN 61..233
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 266..588
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 599 AA; 67696 MW; CD30BC8F7B879FE4 CRC64;
MGWTAKPKAA SWPFKQRLIF ALVIVLLAFS GLIARMIYLQ FHHYETYLGL AEGNRISVQI
IPPERGKIFD RHGQLLAENR SVFSLSFTRE RIPNLAESII KLTELFPDID QERLEQFSQR
ITRLPWHQTH IFPISLSDEQ AARFAAHNHQ FPGIQLTARQ KRVYPFGTST AHLIGYVGRI
SEQDTVRIDR ARYRGTDIIG KSGLERFYED ILHGQPGLRR VETNARGRVI RTLEQIPPTP
GQDLHLSVDI RLQQFIEQEL AGRRAAVVAI EPSTGQILAF VSTPSYDANL FVDGISHREY
NALLNDPERP LINRASRGQY PPGSTTKPMT ALGALELGFT TTTERIFDPG HFEFQDRRYH
NWRREGHGWT DLKRSIVESV DTFYYKMSLD MGIDTLHDIL APFGFGARTG VDHPGEQAGI
LPSQAWKRAT HGQAWFRGET IISSIGQGYN LVTPLQLAQA TSILANRGQV IPPHFNQALA
QNSHQLPIRN RQHWEYVIDG MIDSVHTPRG TAWNSGRHIK GYKIAGKTGT AQVFSLNDQE
YREEEIEQHL HNHALFVAFA PAHNPNIAIS IIVENGGGGG RTAAPIAIRA IDYYQRELQ
//
