ID A0A0A1MU18_9BACI Unreviewed; 356 AA.
AC A0A0A1MU18;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:CEI82416.1};
GN Name=vanY {ECO:0000313|EMBL:CEI82416.1};
GN ORFNames=BN997_02282 {ECO:0000313|EMBL:CEI82416.1};
OS Oceanobacillus oncorhynchi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=545501 {ECO:0000313|EMBL:CEI82416.1, ECO:0000313|Proteomes:UP000040453};
RN [1] {ECO:0000313|EMBL:CEI82416.1, ECO:0000313|Proteomes:UP000040453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oc5 {ECO:0000313|EMBL:CEI82416.1,
RC ECO:0000313|Proteomes:UP000040453};
RA Urmite Genomes Urmite Genomes;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CDGG01000001; CEI82416.1; -; Genomic_DNA.
DR RefSeq; WP_042532226.1; NZ_CDGG01000001.1.
DR AlphaFoldDB; A0A0A1MU18; -.
DR STRING; 545501.BN997_02282; -.
DR OrthoDB; 9792074at2; -.
DR Proteomes; UP000040453; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd14852; LD-carboxypeptidase; 1.
DR Gene3D; 3.30.1380.10; -; 1.
DR Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR InterPro; IPR003709; Pept_M15B.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR PANTHER; PTHR34385; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR34385:SF1; PEPTIDOGLYCAN L-ALANYL-D-GLUTAMATE ENDOPEPTIDASE CWLK; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR Pfam; PF02557; VanY; 1.
DR SUPFAM; SSF55166; Hedgehog/DD-peptidase; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000313|EMBL:CEI82416.1};
KW Hydrolase {ECO:0000313|EMBL:CEI82416.1};
KW Protease {ECO:0000313|EMBL:CEI82416.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000040453}.
FT DOMAIN 76..130
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 205..333
FT /note="Peptidase M15B"
FT /evidence="ECO:0000259|Pfam:PF02557"
FT REGION 23..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 356 AA; 39874 MW; C2C2C357C62E9050 CRC64;
MRGVSWIILS AICFVLIGCG PHEPSPSQED APASEQSAPE EQKDTDDKQA EGQQTEEPEQ
EETEPPDAVL QKFDTDDAVL QLKQALNAIG YDLEATDEFD EELTWAITDF QLQTDDTAIS
GVYDKATREE LLLYYENEKS IEPGEGLAPP PEEPEVTEAG TEVVGNPYDE LSLVNKSFAL
PDDYIPEDLI VPDVPFPFTE DLPKKYLREN AAHALEELFE GAEEAGLEMF AQSGYRSYDR
QDDIFAANAA QNGEDYANTY SARPGESEHQ TGLAMDVTSA EVNLELVEAF GETEEGQWLA
ENAPEYGFII RFPKGKEDIT GYQYEPWHLR YVGEKTAKYI TEQGITLEEY YEEQAE
//
