ID D6YS23_WADCW Unreviewed; 426 AA.
AC D6YS23;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Putative D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:ADI38868.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:ADI38868.1};
GN Name=dacC {ECO:0000313|EMBL:ADI38868.1};
GN OrderedLocusNames=wcw_1519 {ECO:0000313|EMBL:ADI38868.1};
OS Waddlia chondrophila (strain ATCC VR-1470 / WSU 86-1044).
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Waddliaceae; Waddlia.
OX NCBI_TaxID=716544 {ECO:0000313|EMBL:ADI38868.1, ECO:0000313|Proteomes:UP000001505};
RN [1] {ECO:0000313|EMBL:ADI38868.1, ECO:0000313|Proteomes:UP000001505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-1470 / WSU 86-1044 {ECO:0000313|Proteomes:UP000001505};
RX PubMed=20531937; DOI=10.1371/journal.pone.0010890;
RA Bertelli C., Collyn F., Croxatto A., Ruckert C., Polkinghorne A.,
RA Kebbi-Beghdadi C., Goesmann A., Vaughan L., Greub G.;
RT "The Waddlia genome: a window into chlamydial biology.";
RL PLoS ONE 5:E10890-E10890(2010).
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DR EMBL; CP001928; ADI38868.1; -; Genomic_DNA.
DR RefSeq; WP_013182576.1; NZ_LVEB01000002.1.
DR AlphaFoldDB; D6YS23; -.
DR STRING; 716544.wcw_1519; -.
DR KEGG; wch:wcw_1519; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_027070_7_3_0; -.
DR OrthoDB; 9791132at2; -.
DR Proteomes; UP000001505; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.60.410.10; D-Ala-D-Ala carboxypeptidase, C-terminal domain; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR037167; Peptidase_S11_C_sf.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR21581:SF34; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACC; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000313|EMBL:ADI38868.1};
KW Hydrolase {ECO:0000313|EMBL:ADI38868.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:ADI38868.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001505};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 397..415
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..270
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
SQ SEQUENCE 426 AA; 47918 MW; 2B1E92EA3B8F8D49 CRC64;
MNSTFCLIFA LLLANSILNG IEIKIHADSA ILMNADTGAI LYEKNGKKEH FPASLTKIAT
AIYTLQLREQ KLDKMLTAEH EAIASVSEEE MVRSNYSLPA YWLTRGTSHI GIKKGEELSL
RDLLYGMMVA SGGDASNMIA LYMGGTIPVF MEELNLYLKE LGCTSTYLMN PHGLHHPRHV
STAYDMAVLT REALKNSTFR EIVKTVRCQR PETNKQKATT LIQTNRLLRK GKYYYSKAIG
VKTGYTSQAK NNLVAAAKDG DRTLIAVFMH CDDREKMFLD AKQLFNKAFK EEKISRKVFQ
AGPQKMTLRV EGAAKSIATY IKNDVVFDFY PSEEPKLKCL LKWNAVSLPV QKDQQVGVLV
FEDDNGKELH SEALFAKEKV DHHFFRRLRD RITGRKILKF FGACLAVLFI GGLIYELGCV
KKSSSG
//
