ID A0A0F5MS03_9MYCO Unreviewed; 458 AA.
AC A0A0F5MS03;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 13-SEP-2023, entry version 30.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KKB97535.1};
GN ORFNames=WR43_18720 {ECO:0000313|EMBL:KKB97535.1};
OS Mycolicibacter arupensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacter.
OX NCBI_TaxID=342002 {ECO:0000313|EMBL:KKB97535.1, ECO:0000313|Proteomes:UP000034416};
RN [1] {ECO:0000313|Proteomes:UP000034416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GUC1 {ECO:0000313|Proteomes:UP000034416};
RA Greninger A.L., Cunningham G., Chiu C.Y., Miller S.;
RT "Genome sequence of Mycobacterium arupense GUC1.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKB97535.1}.
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DR EMBL; LASW01000126; KKB97535.1; -; Genomic_DNA.
DR RefSeq; WP_046191112.1; NZ_VUJZ01000002.1.
DR AlphaFoldDB; A0A0F5MS03; -.
DR STRING; 342002.BST15_10580; -.
DR PATRIC; fig|342002.3.peg.3270; -.
DR OrthoDB; 56883at2; -.
DR Proteomes; UP000034416; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000667; Peptidase_S13.
DR NCBIfam; TIGR00666; PBP4; 2.
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.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:KKB97535.1};
KW Hydrolase {ECO:0000313|EMBL:KKB97535.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:KKB97535.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 458 AA; 46619 MW; 3E83E36DDB3CB6F4 CRC64;
MQPTRWRHSG AHLGIAAAVL ALAAAVVVVA VAVLPDESGA GARVVSPAPV ATAKPGVVPV
SEDAAVPAGS ALAAALAPAL ADPNLGRLTG RITDALTGKA LWTQQEDLPM QPASTNKVLT
AAAALLALDP SARVTTRVTA SDQPGVVVLV GDGDPTLSTA EVGQDTWYRE AARISDLADQ
VRRSGVEVSE VQVDISAFTG PTMAQGWDAE DIEGGDIAPI EAVMVDGGRV QPTTVESRRS
TTPALDAGKA LAAELGVDPD QVSIVSSSVT GRELGAVRSA PLVVRLGEMM NASDNVMAES
IAREVAAAMG RPRSFAGAVD AVINRLATAH IAVSGASLQD ASGLSVDDRL SARTLDSVVQ
AAAGPDLPEL RPLLDMLPVA GGSGTLSERF LNPKTGRGAA GWLRAKTGSL TRTNALAGIV
TDRDQRVLTF AFISNDAGPT GRTAIDALAA VLRTCGCR
//
