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Database: UniProt
Entry: M2XF21_9MICC
LinkDB: M2XF21_9MICC
Original site: M2XF21_9MICC 
ID   M2XF21_9MICC            Unreviewed;       250 AA.
AC   M2XF21;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:EME37716.1};
GN   ORFNames=C884_01090 {ECO:0000313|EMBL:EME37716.1};
OS   Kocuria palustris PEL.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=1236550 {ECO:0000313|EMBL:EME37716.1, ECO:0000313|Proteomes:UP000009877};
RN   [1] {ECO:0000313|EMBL:EME37716.1, ECO:0000313|Proteomes:UP000009877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEL {ECO:0000313|EMBL:EME37716.1,
RC   ECO:0000313|Proteomes:UP000009877};
RX   PubMed=24504000;
RA   Sharma G., Khatri I., Subramanian S.;
RT   "Draft Genome Sequence of Kocuria palustris PEL.";
RL   Genome Announc. 2:e01261-13(2014).
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:EME37716.1}.
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DR   EMBL; ANHZ02000002; EME37716.1; -; Genomic_DNA.
DR   RefSeq; WP_006213474.1; NZ_ANHZ02000002.1.
DR   AlphaFoldDB; M2XF21; -.
DR   STRING; 71999.KPaMU14_09745; -.
DR   Proteomes; UP000009877; 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   InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR   InterPro; IPR003709; Pept_M15B.
DR   PANTHER; PTHR34385; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR34385:SF1; PEPTIDOGLYCAN L-ALANYL-D-GLUTAMATE ENDOPEPTIDASE CWLK; 1.
DR   Pfam; PF02557; VanY; 1.
DR   SUPFAM; SSF55166; Hedgehog/DD-peptidase; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:EME37716.1};
KW   Hydrolase {ECO:0000313|EMBL:EME37716.1};
KW   Protease {ECO:0000313|EMBL:EME37716.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009877};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..250
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038965586"
FT   DOMAIN          95..222
FT                   /note="Peptidase M15B"
FT                   /evidence="ECO:0000259|Pfam:PF02557"
FT   REGION          24..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   250 AA;  26631 MW;  32E23B9D596F9CE5 CRC64;
     MTTPLPRRLA ASVTLLGLLG LSACGSEQPQ EDSSSSAAAD SAQSGGAEAE AESGAAAVSD
     ADVDTSTSTD VVVNKARPLD PEDYAPEPLE DIEGQQLRED AAGAAQQMLS DMRDEGITVS
     ITSAYRPYDE QVTTYQHWVD VNGQETADTI SARPGHSEHQ TGLVMDIADG SGCDLQECFA
     DTAAAQWAAE HAQDYGFVLR YPQDGEDVTG YAYEPWHFRY IGEERAQEFA DSGAATLEEF
     YGTGPAPDYS
//
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