ID A0A1E5AG05_9RHOB Unreviewed; 498 AA.
AC A0A1E5AG05;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:OED49039.1};
GN ORFNames=AB838_08755 {ECO:0000313|EMBL:OED49039.1};
OS Rhodobacteraceae bacterium (ex Bugula neritina AB1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1868286 {ECO:0000313|EMBL:OED49039.1, ECO:0000313|Proteomes:UP000094333};
RN [1] {ECO:0000313|EMBL:OED49039.1, ECO:0000313|Proteomes:UP000094333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB1-7 {ECO:0000313|EMBL:OED49039.1};
RX PubMed=27681823; DOI=10.1038/srep34362;
RA Miller I.J., Weyna T.R., Vanee N., Fong S., Lim-Fong G.E.;
RT "Single sample resolution of rare microbial dark matter in a marine
RT invertebrate metagenome.";
RL Sci. Rep. 6:34362-34362(2016).
CC -!- SIMILARITY: Belongs to the peptidase S13 family.
CC {ECO:0000256|ARBA:ARBA00006096}.
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:OED49039.1}.
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DR EMBL; MDLF01000058; OED49039.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E5AG05; -.
DR STRING; 1868286.AB838_08755; -.
DR Proteomes; UP000094333; Unassembled WGS sequence.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.50.80.20; D-Ala-D-Ala carboxypeptidase C, peptidase S13; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000667; Peptidase_S13.
DR InterPro; IPR006311; TAT_signal.
DR NCBIfam; TIGR00666; PBP4; 1.
DR PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR Pfam; PF02113; Peptidase_S13; 1.
DR PRINTS; PR00922; DADACBPTASE3.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:OED49039.1};
KW Hydrolase {ECO:0000313|EMBL:OED49039.1};
KW Protease {ECO:0000313|EMBL:OED49039.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..498
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009170422"
SQ SEQUENCE 498 AA; 52534 MW; 9EA270D294EC033E CRC64;
MNKMTSRRTF LLSGLAALAG TSALANAPAV SLRPVARKVS SLAAGADGLQ ALIERAGLRG
KAVCAVADVK TGQMLETAGG TQALPPASVA KALTALYALD VLGADHRFET RILATGGVSG
GVVAGDVILA GGGDPLLNSD HLALLAKSLK TAGVREVRGK FLVWDGALPS VKTIDPDQPD
HVGYSPAVSG ISLNFNRVHF EWKRAAGGGW VTTMDARTEK YRPEVAAARM AIQTRAVPVY
TYAEKGGVDH WTVASKALGK GGSRWLPVRN PAAYAGDVFR TMARANGISL PKARKTKSLP
SATLLAQHRS PPLDVLLKAM LKYSNNLMAE MIGMSATAAR AGRPASLSAS AAEMSRWAAA
KYGMSSTRLV DHSGLGEDSR MTPADLTGAL VAAYKAGQLK PLLKSFQMRD AKGRIIKGHP
IKVAAKTGTL NFVSGLGGFM TAADGTVLAF AIFTADQKTR DRLTRAQRER PQGARSWNRR
AKQLQQQLIE RWGAVYGS
//
