ID A0A078AZ93_STYLE Unreviewed; 550 AA.
AC A0A078AZ93;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase A N-terminal domain-containing protein {ECO:0000259|Pfam:PF00768};
GN Name=Contig12655.g637 {ECO:0000313|EMBL:CDW86133.1};
GN ORFNames=STYLEM_15224 {ECO:0000313|EMBL:CDW86133.1};
OS Stylonychia lemnae (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW86133.1, ECO:0000313|Proteomes:UP000039865};
RN [1] {ECO:0000313|EMBL:CDW86133.1, ECO:0000313|Proteomes:UP000039865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=130c {ECO:0000313|EMBL:CDW86133.1,
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; CCKQ01014378; CDW86133.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078AZ93; -.
DR EnsemblProtists; CDW86133; CDW86133; STYLEM_15224.
DR InParanoid; A0A078AZ93; -.
DR OrthoDB; 5622425at2759; -.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000039865};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 243..348
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT DOMAIN 379..501
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 550 AA; 63599 MW; 67BFC9BFD83F1B2F CRC64;
MEIKKEQPQP LIGKARIHSS RLPPTYGMIS NKYTLGGQER IGRHPNSRKI SLPSQYPSLQ
RSSTQSRQNS LVDNQQSNQS HNRSQANSSQ RERPFRIGRH FEKENSFNIN QLPILEESGS
LEKTMKEMFI NGDKFGIKNQ KYKQPLNQYN QQQQQIYMSL QQQQQQMQPQ QCKTPTCIQS
RALEPIQFDQ NIPRKEQAVI EQQNVSVNFQ RNRNNSNSAI FKHQQFKKNY VKKLNSFNVY
LPPPQVTAKC WAIFDASKMN FIHGKREYMR REVASLTKMM TAYTVIKLVK EYKIDMSKEM
VVIQQVAAQI SGTTACLQEA DQLTVEQLLY GLMLPSGNDA AFALAQHFGQ ILFNSNYESL
EEGNKVYSYQ FNWHGYYVKY FLREMNENAA RIQMMSTNFD SPHGLMNQQN YSTAYDIAKL
ASKCMQNDLY RKIVNTKIFE CQGRTKDGQL RKYCWENTNK LLGQDGFNGI KTGITDSAGP
CLASSYQKGP DFFIVVILNS KSMEQRWVEV PKLVEWAITK KNAQIEMSKQ YDLGNTDSNH
SLVSQKLNLR
//
