ID   W4HNF0_9RHOB            Unreviewed;       501 AA.
AC   W4HNF0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:ETW13646.1};
GN   ORFNames=ATO8_06436 {ECO:0000313|EMBL:ETW13646.1};
OS   Roseivivax marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseivivax.
OX   NCBI_TaxID=1379903 {ECO:0000313|EMBL:ETW13646.1, ECO:0000313|Proteomes:UP000019063};
RN   [1] {ECO:0000313|EMBL:ETW13646.1, ECO:0000313|Proteomes:UP000019063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22II-s10s {ECO:0000313|EMBL:ETW13646.1,
RC   ECO:0000313|Proteomes:UP000019063};
RX   PubMed=24567080; DOI=10.1007/s10482-014-0140-5;
RA   Li G., Lai Q., Liu X., Sun F., Shao Z.;
RT   "Roseivivax atlanticus sp. nov., isolated from surface seawater of the
RT   Atlantic Ocean.";
RL   Antonie Van Leeuwenhoek 105:863-869(2014).
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:ETW13646.1}.
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DR   EMBL; AQQW01000003; ETW13646.1; -; Genomic_DNA.
DR   RefSeq; WP_043843018.1; NZ_AQQW01000003.1.
DR   AlphaFoldDB; W4HNF0; -.
DR   STRING; 1379903.ATO8_06436; -.
DR   PATRIC; fig|1317118.6.peg.1333; -.
DR   eggNOG; COG2027; Bacteria.
DR   Proteomes; UP000019063; 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:ETW13646.1};
KW   Hydrolase {ECO:0000313|EMBL:ETW13646.1};
KW   Protease {ECO:0000313|EMBL:ETW13646.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019063};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..501
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004843229"
SQ   SEQUENCE   501 AA;  53240 MW;  988A218DDA7223AD CRC64;
     MTAPLTRRRL LAALAATTAA APAFANAPET SLRPLARGED FFKRAVPTLD EIASAANLDG
     FLGCAVGNTE TGELLEDLNG AEGLPPASVA KALTASYALE HLGPDHRFVT RLLTSGEVSE
     DGTLDGDLIL AGGADPTLDT DGLAALAGDL RDAGVSSVTG RLLVWGGALP EVPAIDPGQP
     DHVGYNPSVA GLNLNYNRVH FEWQRAGEGY QVAMDGRSDS LRPPVHMARM VVVARRTPVY
     TYHDGDARDE WTVAKSALGN AGSRWLPVRR PTLYAGEVFQ AVAGSNGLRL KSPEVVDTLP
     EDARELARRE SQPLTDILQD MLKWSTNLTA EVVGCAATAA ATGSVPASLE ASAAELNGWA
     EAELGVTGIA LVDHSGLGED SRVAPVAMTR ALIALRERLD LKPILKPIPM RDDARRILSN
     HPLDVHAKTG TLNFVSGLAG YIDCPDGTEL AFAIFSGDLD HRATIAREDR EGPPGARTYN
     TRAKKWQMEL IKRWGTVYGT A
//