ID A0A429XE51_9BACI Unreviewed; 682 AA.
AC A0A429XE51;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000256|ARBA:ARBA00012448};
DE EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN ORFNames=D5F11_000730 {ECO:0000313|EMBL:RST61748.1};
OS Siminovitchia terrae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Siminovitchia.
OX NCBI_TaxID=1914933 {ECO:0000313|EMBL:RST61748.1, ECO:0000313|Proteomes:UP000287296};
RN [1] {ECO:0000313|EMBL:RST61748.1, ECO:0000313|Proteomes:UP000287296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29736 {ECO:0000313|EMBL:RST61748.1,
RC ECO:0000313|Proteomes:UP000287296};
RA Sun L., Chen Z.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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;
CC Evidence={ECO:0000256|ARBA:ARBA00034000};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RST61748.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QYTW02000001; RST61748.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A429XE51; -.
DR OrthoDB; 9770103at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000287296; Unassembled WGS sequence.
DR GO; GO:0016020; C: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-EC.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
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 Gene3D; 1.10.10.1230; Penicillin-binding protein, N-terminal non-catalytic domain, head sub-domain; 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 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 Membrane {ECO:0000256|ARBA:ARBA00023136}.
FT DOMAIN 45..276
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 325..643
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 682 AA; 76832 MW; 425654EFEBAF626B CRC64;
MNMLFFIVFL LFSLLILRLG VIQIVYGEDA KREVERTEDI TVNKSVPRGK IYDRKHRLIV
DNEPRKAITY TIPNQFDQKE TLKTAKALAK LINKDTDKIT ERDKIDYWLM THPDEAAKKV
SKAELEKYKD KTNELYKLQL ERVTKEEIAS LTQEDLEVLA IYREFTGGYA LTQQIVKNED
VSTEEYAKVS ERLAELPGVD TTTDWERKYA YEDTLRSILG NVSNGLPSEK TDYYMSRGYS
RNDRVGKSYI ELQYEDVLRG QKEKVKNITR SGTVIESKVL HEGQRGKDLV LTVDMELQHE
VDKIVEEELR KTKMRGGTGL LDRAFVTLMD PHTGEILAMS GKQYAYDEDE GRYKFSDFAA
GNFTTSYVVG SSVKGASVLT GYMTGVITLG NNTLLDEPLL IKGSPSKSSH FNRGGYVYLN
DHTALVRSSN VYMFKLAIAI GDGQYRRNQS LIIDKEKAFR EMREHFSQFG LGIRTGIDLP
GEQIGFRGSV EEAHGGNVLD FAIGQYDSYT PLQLAQYVST IANGGYRMQP HIVKEIRDPG
EDKEEMGSLA QEVQPKVLNR INAEDAWIKR VQGGFWGVFH EANGTGKAFA SEPYSPAGKT
GTAETVDRGT GVWNLSLVAY APYENPEVAM SIVVPSAYVK GGSPNNINSD IGKRVLKAYF
DLKNKKDDTA SEETNEDVEE QE
//
