PSCA_DICDI
ID PSCA_DICDI Reviewed; 522 AA.
AC Q86I79; Q55AF7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Penicillin-sensitive carboxypeptidase A;
DE EC=3.4.16.4;
GN Name=pscA; ORFNames=DDB_G0271902;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP DISRUPTION PHENOTYPE, ACTIVITY REGULATION, AND FUNCTION.
RX PubMed=12843630; DOI=10.1248/bpb.26.1018;
RA Yasukawa H., Kuroita T., Tamura K., Yamaguchi K.;
RT "Identification of a penicillin-sensitive carboxypeptidase in the cellular
RT slime mold Dictyostelium discoideum.";
RL Biol. Pharm. Bull. 26:1018-1020(2003).
CC -!- FUNCTION: Carboxypeptidase. {ECO:0000269|PubMed:12843630}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC -!- ACTIVITY REGULATION: Inhibited by penicillin G.
CC {ECO:0000269|PubMed:12843630}.
CC -!- DISRUPTION PHENOTYPE: Not essential for cell growth.
CC {ECO:0000269|PubMed:12843630}.
CC -!- MISCELLANEOUS: Since D.discoideum amoebae do not have a peptidoglycan
CC cell wall, the function is not known.
CC -!- SIMILARITY: Belongs to the peptidase S13 family. {ECO:0000305}.
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DR EMBL; AAFI02000007; EAL71475.1; -; Genomic_DNA.
DR RefSeq; XP_645397.1; XM_640305.1.
DR AlphaFoldDB; Q86I79; -.
DR SMR; Q86I79; -.
DR STRING; 44689.DDB0233864; -.
DR MEROPS; S13.A01; -.
DR PaxDb; Q86I79; -.
DR EnsemblProtists; EAL71475; EAL71475; DDB_G0271902.
DR GeneID; 8618223; -.
DR KEGG; ddi:DDB_G0271902; -.
DR dictyBase; DDB_G0271902; pscA.
DR eggNOG; ENOG502S3R5; Eukaryota.
DR HOGENOM; CLU_017692_1_2_1; -.
DR InParanoid; Q86I79; -.
DR OMA; DGTMRKR; -.
DR PhylomeDB; Q86I79; -.
DR PRO; PR:Q86I79; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IDA:dictyBase.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IBA:GO_Central.
DR GO; GO:0030163; P:protein catabolic process; IDA:dictyBase.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; -; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000667; Peptidase_S13.
DR PANTHER; PTHR30023; PTHR30023; 1.
DR Pfam; PF02113; Peptidase_S13; 1.
DR PRINTS; PR00922; DADACBPTASE3.
DR SUPFAM; SSF56601; SSF56601; 1.
DR TIGRFAMs; TIGR00666; PBP4; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase; Hydrolase; Protease; Reference proteome.
FT CHAIN 1..522
FT /note="Penicillin-sensitive carboxypeptidase A"
FT /id="PRO_0000385367"
FT ACT_SITE 94
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P39844"
FT ACT_SITE 97
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P39844"
FT ACT_SITE 351
FT /evidence="ECO:0000250|UniProtKB:P39844"
FT BINDING 461
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 522 AA; 56873 MW; 7A9744141131205A CRC64;
MKNYKIITLL LIISILFNII RSNKISLKDS DSGSNGNQDI QILINDILNN CSSSESSSCF
GTQWGVVADI YTPSNGEFTN IFSLNELQAF TPASNTKLFT TISIFYTFGE DFKVFTPFFT
DKPFNSVSGG SSNSELDFIC VKGMGDPSMS IDNLIEAAKF FSSNPTMKKV NKLLLDTSFY
NIGNGVDGNI PSAWEWEDLT STYGSIPTPL IINENTMDIY ITPSNVIGGK PTASFKYSGE
DKYLPVIILA TTTTTSNSST STLNYSFKMS SQSIYITGNC DINGGIQIIT VPILDPEQYF
LTVFSALLED GGVEISQTAI GSCNYTGMDY KSFEVISPEL SEMLNYTLLT SNNLYAETFL
RQMGTFNSAA SESTPTYQAG LEYIQQTLSI PTSLYTQVDG SGLSRNNFIT PKSLITVIEN
VYTNVGDPQH DYISYLPVAS LSGTLSKRFI NTPASGIVHA KTGSMTGVNS LTGVILPNGL
SDDQQNSIFF SIIANNSPAQ NTDIIDIIDQ IVILLTKFIL SS
