ID F4XND8_9CYAN Unreviewed; 451 AA.
AC F4XND8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:EGJ34197.1};
GN ORFNames=LYNGBM3L_24050 {ECO:0000313|EMBL:EGJ34197.1};
OS Moorena producens 3L.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Moorena.
OX NCBI_TaxID=489825 {ECO:0000313|EMBL:EGJ34197.1, ECO:0000313|Proteomes:UP000003959};
RN [1] {ECO:0000313|Proteomes:UP000003959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3L {ECO:0000313|Proteomes:UP000003959};
RX PubMed=21555588; DOI=10.1073/pnas.1101137108;
RA Jones A.C., Monroe E.A., Podell S., Hess W.R., Klages S., Esquenazi E.,
RA Niessen S., Hoover H., Rothmann M., Lasken R.S., Yates J.R.III.,
RA Reinhardt R., Kube M., Burkart M.D., Allen E.E., Dorrestein P.C.,
RA Gerwick W.H., Gerwick L.;
RT "Genomic insights into the physiology and ecology of the marine filamentous
RT cyanobacterium Lyngbya majuscula.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:8815-8820(2011).
CC -!- SIMILARITY: Belongs to the peptidase S13 family.
CC {ECO:0000256|ARBA:ARBA00006096}.
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DR EMBL; GL890840; EGJ34197.1; -; Genomic_DNA.
DR RefSeq; WP_008181373.1; NZ_MKZR01000001.1.
DR AlphaFoldDB; F4XND8; -.
DR eggNOG; COG2027; Bacteria.
DR HOGENOM; CLU_047821_0_0_3; -.
DR OrthoDB; 9802627at2; -.
DR Proteomes; UP000003959; 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 PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR Pfam; PF02113; Peptidase_S13; 2.
DR PRINTS; PR00922; DADACBPTASE3.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:EGJ34197.1};
KW Hydrolase {ECO:0000313|EMBL:EGJ34197.1};
KW Protease {ECO:0000313|EMBL:EGJ34197.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..451
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003321181"
FT REGION 28..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 48147 MW; ABED3D22F43B3816 CRC64;
MLKTKTYVTG TLSTLLLALV IGCNGADSPK GVSPSPDPES SQSSEPENAL KVIPKPDQPL
TVAETNPIPG SQQSVDQYLK GLSAKGMTKT NQGIWIESGD TLLANHQGTI PLPAASLTKA
ATTLAALSTF GPDHQFITQF SATGPIENGV LQGDLVVQGS EDPFFVWEEA IAVGNQLNQL
GIKQVTGNLV IVGKFYMNFE TLPLKAGTLL KQGLNGKSWP PAAETQYQTL PPGTPRPEIA
IAGSVQVVAS PPDNLQPLVR QYSFPLAELL KKMNRYSNNK MADMLANTAG GAKVVARKAA
EAAGVPQSEI SLINGSGLGE ENRMSPRAVT AVFLAIERYL KQYNMTVADV FAIVGQDKGI
LNERPLPNLA VVKSGSLNYV STLAGALPTQ TYGTVWFAVM NSGGDYTKYR TQQEVLLKEL
VTKWGVVQSV PSDIKPSPQR IGKRSFSEIV R
//
