ID A0A078B7C1_STYLE Unreviewed; 565 AA.
AC A0A078B7C1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=D-alanyl-d-alanine carboxypeptidase family protein {ECO:0000313|EMBL:CDW90106.1};
GN Name=Contig1647.g1794 {ECO:0000313|EMBL:CDW90106.1};
GN ORFNames=STYLEM_19246 {ECO:0000313|EMBL:CDW90106.1};
OS Stylonychia lemnae (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW90106.1, ECO:0000313|Proteomes:UP000039865};
RN [1] {ECO:0000313|EMBL:CDW90106.1, ECO:0000313|Proteomes:UP000039865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=130c {ECO:0000313|EMBL:CDW90106.1,
RC ECO:0000313|Proteomes:UP000039865};
RA Swart Estienne;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164}.
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DR EMBL; CCKQ01018170; CDW90106.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078B7C1; -.
DR EnsemblProtists; CDW90106; CDW90106; STYLEM_19246.
DR InParanoid; A0A078B7C1; -.
DR OrthoDB; 179548at2759; -.
DR Proteomes; UP000039865; Unassembled WGS sequence.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR21581:SF32; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACB; 1.
DR Pfam; PF00768; Peptidase_S11; 2.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:CDW90106.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000313|EMBL:CDW90106.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000039865};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 251..354
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT DOMAIN 401..522
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 146..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 565 AA; 64335 MW; 73E22F3C7EE4FFFE CRC64;
MMTSSGRKDS HKYIKISSQP LQYSLDNSLN YSTTKKRDST FDSEASYFKS VNPGDSYLRK
TQLSSLNKLQ GNPNMSGLEQ ESINASFNLI NINSLELTPI KRQNIPTRII TQRNTVRISQ
NTQIRVSNKI HLDDEISNNN KIQQIQNKST SIQSSSTQAS STTNSSNQST SSHQSSIATG
QVCIIPKDKI NFVSNVVLAD PKNQTQTNLK SNHFQLIRRK KKKSLSTSIS CRPSSSEQLM
HKQLLLDNPA PFVSAQSWAM IDKSSGELIF GRNEQESRQV ASLTKIMTSY VVLDIISRYH
MNEHKTFVKI LPSAVKLIGT TANLLDDDKL TVWELMHGMM LPSGNDAAQS LAIHFGIFCL
KEEYKAHKNL EALDEDKSEI LKLTYDNFQD LEDKPHLVSK ALNEFYRQMN REAMYLNLKN
TNFSSAHGMF HEQNYSSAED IAKLSYFAMK NSLFRQIVKT QKYTCESRVE IGHLYQWQNT
NKLLEMGYSG LKTGITPTAG PCLAASITKN EFKFIIVILN SRSMEHRWLE VQKLVHWAMQ
KITKIKQSDL KPKMKRKLLK KLLHL
//
