ID A0A2N5G5P6_9BACI Unreviewed; 665 AA.
AC A0A2N5G5P6;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=CU633_17940 {ECO:0000313|EMBL:PLR76040.1};
OS Bacillus sp. V3-13.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2053728 {ECO:0000313|EMBL:PLR76040.1, ECO:0000313|Proteomes:UP000234805};
RN [1] {ECO:0000313|EMBL:PLR76040.1, ECO:0000313|Proteomes:UP000234805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V3-13 {ECO:0000313|EMBL:PLR76040.1,
RC ECO:0000313|Proteomes:UP000234805};
RA Seuylemezian A., Cooper K., Vaishampayan P.;
RT "Comparitive Functional Genomics of Dry Heat Resistant strains isolated
RT from the Viking Spacecraft.";
RL Submitted (NOV-2017) 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 -!- 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:PLR76040.1}.
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DR EMBL; PGUZ01000055; PLR76040.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5G5P6; -.
DR OrthoDB; 9766847at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000234805; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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-EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
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 InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR007887; MecA_N.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR30627:SF25; PENICILLIN-BINDING PROTEIN 3; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR Pfam; PF05223; MecA_N; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF54427; NTF2-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000234805};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:PLR76040.1}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..665
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038423684"
FT DOMAIN 25..144
FT /note="NTF2-like N-terminal transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF05223"
FT DOMAIN 153..318
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 353..660
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 665 AA; 73396 MW; CC33C4D10A20DCB5 CRC64;
MRKSIYLFVM VLAAALLAGC NNDPTPEDRF SKYVELWNEQ KFEDMYGYLT ADAKEKVTKK
EYVERYQKVY SDLEISDLEI KFDPPEEKAE GEEAKFSFSA KMNSFAGPIS FKHQAPLKKE
TQKEKENWFV DWDTTFIFPE LEAGDKIGVS SVPSVRGEIF DRNDNGLAVN GTAFEIGIVP
AQMEGSREDI ISRVAGLLGM EAAQIDKALN ADWVQPDYFV PIKKIPMENQ ELLAQLMEIP
SVLKKDVPAR VYPYKDAAAH LVGYVGPVTA EELKELAGKG YSSNDVIGKR GMEQVLEERL
KGQNGAKIYI KKEDGSEVQL AEKEVVNGEN IKLTIDIDLQ SKMFNELAGE AGAGTAMNPV
TGETLALVSS PAFDPNTIAL GATGQYWQSI EEHPQKPLTT RFKQTYAPGS VMKPITAVIG
LKEGAITPEQ QMEVDGLQWQ KDNSWGSYKI TRVTDPNGPV NLDRALLLSD NIYFAQAALA
IGAEKFTAGL KSFGFEEDFA YPFPLEASKI GELDNEIRLA DSGYGQGHIE MSIVHLASTY
TPFVNNGTMI KPILLAEEKT AQPWKENLVD QTAVTQINNS LRKVVEDPSG TANSARIDGY
PLAGKTGTAE LKEKQGEKGT ENGWFVAYNV ENPNLLIAMM VEGVENKGGS KAVVSRVKNV
FQSRQ
//
