ID A0A0M4NXL9_9GAMM Unreviewed; 616 AA.
AC A0A0M4NXL9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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 ORFNames=SP60_06120 {ECO:0000313|EMBL:ALE52814.1};
OS Candidatus Thioglobus autotrophicus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Thioglobus.
OX NCBI_TaxID=1705394 {ECO:0000313|EMBL:ALE52814.1, ECO:0000313|Proteomes:UP000058020};
RN [1] {ECO:0000313|EMBL:ALE52814.1, ECO:0000313|Proteomes:UP000058020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EF1 {ECO:0000313|EMBL:ALE52814.1,
RC ECO:0000313|Proteomes:UP000058020};
RX PubMed=26494660;
RA Shah V., Morris R.M.;
RT "Genome Sequence of 'Candidatus Thioglobus autotrophica' Strain EF1, a
RT Chemoautotroph from the SUP05 Clade of Marine Gammaproteobacteria.";
RL Genome Announc. 3:e01156-15(2015).
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; CP010552; ALE52814.1; -; Genomic_DNA.
DR RefSeq; WP_053951783.1; NZ_CP010552.1.
DR AlphaFoldDB; A0A0M4NXL9; -.
DR STRING; 1705394.SP60_06120; -.
DR KEGG; tho:SP60_06120; -.
DR PATRIC; fig|1705394.5.peg.1219; -.
DR OrthoDB; 9766847at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000058020; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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|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:UP000058020};
KW Transferase {ECO:0000313|EMBL:ALE52814.1};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02081}.
FT TRANSMEM 20..37
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
FT DOMAIN 61..231
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 263..602
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT ACT_SITE 322
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
SQ SEQUENCE 616 AA; 68801 MW; F39393E619D5A7D8 CRC64;
MDSISNTQLE NTLLSSRLKL ALVFIFLLTL LLLVRIYNLQ VVHHEYYQEE SLGNQMRTLP
IIPSRGKIFD RNGQILATNK LTYQLTLTPE KVGNISKTLI GLEKQGFIDQ EDIQLYYKNR
KRFRKFHNIP VKLNLSEQQV AKFLVSNQFP GVDIEPYFHR VYPHNASSVH ALGYVSRMSK
KDKALYDKRN YSGTLFVGKV GIEKQYESLL HGQTGLKQIE RNVSGRVIDT QIITPAIAGQ
NLYLSLDLDM QKKAEELLKG KRGAIVAIDT RNGEVLALVS TPIYNPNWFV NGISHANYNS
LQSSSDIPQL NRTVQGLYPP ASTIKPMVAL AGLEQGTIDN QSSVFDRGYY QLPGVKRKFH
NWDRNGHGRV NVTDAIARSN DVFFYDLANK MGIDNLHNGL NLFNFGQKTG IDIPGEQGGI
LPSKSWKKIN KNEPWYKGET LNTGIGQGFM TSSPLQLAVA TAALANKGQL LKPILLKNTQ
LLGQSITEVK KAVGRQIPIH DIKNWETVID GMRQVIYSPK GTARRLNNKL GYTLAGKTGT
AQVFGLDAEE VYIAEKLEEK LRDHALFTGF APIENPQIAI AVVVENAGSG SSKAAPLARQ
VLDVYFNKHL DNELAQ
//
