ID Q05SX9_9SYNE Unreviewed; 442 AA.
AC Q05SX9;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Putative D-Ala-D-Ala carboxypeptidase 3 (S13) family protein {ECO:0000313|EMBL:EAU73824.1};
GN ORFNames=RS9916_29984 {ECO:0000313|EMBL:EAU73824.1};
OS Synechococcus sp. RS9916.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=221359 {ECO:0000313|EMBL:EAU73824.1, ECO:0000313|Proteomes:UP000004972};
RN [1] {ECO:0000313|EMBL:EAU73824.1, ECO:0000313|Proteomes:UP000004972}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS9916 {ECO:0000313|EMBL:EAU73824.1,
RC ECO:0000313|Proteomes:UP000004972};
RA Scanlan D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (OCT-2006) 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:EAU73824.1}.
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DR EMBL; AAUA01000002; EAU73824.1; -; Genomic_DNA.
DR RefSeq; WP_007097931.1; NZ_DS022299.1.
DR AlphaFoldDB; Q05SX9; -.
DR STRING; 221359.RS9916_29984; -.
DR eggNOG; COG2027; Bacteria.
DR HOGENOM; CLU_051019_0_0_3; -.
DR OrthoDB; 9802627at2; -.
DR Proteomes; UP000004972; Unassembled WGS sequence.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000667; Peptidase_S13.
DR NCBIfam; TIGR00666; PBP4; 1.
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.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:EAU73824.1};
KW Hydrolase {ECO:0000313|EMBL:EAU73824.1};
KW Protease {ECO:0000313|EMBL:EAU73824.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004972};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..442
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004164764"
SQ SEQUENCE 442 AA; 47113 MW; 59AB0F6C74CEEFB2 CRC64;
MKPNALSPPL VALIIAGLAA PSWAQARKTK LQEALAEGVE PAVSVPLLTP PPPASNRALP
TLQLGRVCAP LQASLLRSLG RSKAAWSVSV VDPNGALIGD VNGGLPRVPA SNQKLITTAF
ALDRLGPDFR LKTKLLRRPD GTMEITGEGD PDLGLVGVQR FAMAALGQGG ARAAKGGQVQ
LLLREEPQQR WWPRDWHPAD RVEAYGAPIT RLALTSNALG RAIRNPAARF QTLLQREIER
QGGNVRMGVK PPLVSQTGAD TGVVVLHEES SAPMHALLSL ANTESHNFTA EVLLREAADQ
WNLSQASVSA MQWMRAQNLP TAGLRVADGS GLSRGNRVTS RTLAALLLRM NQHPLSAYYR
SSMAIAGQRG TLRNYFRGSN LEGRFHGKTG TLTGVRSVSG ILQTKDGLRF VSMISNGAPA
PNATIGQVLR SVQQLSPCPS ST
//
