ID A0A139WUV9_9CYAN Unreviewed; 446 AA.
AC A0A139WUV9;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KYC36221.1};
GN ORFNames=WA1_41570 {ECO:0000313|EMBL:KYC36221.1};
OS Scytonema hofmannii PCC 7110.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC Scytonema.
OX NCBI_TaxID=128403 {ECO:0000313|EMBL:KYC36221.1, ECO:0000313|Proteomes:UP000076925};
RN [1] {ECO:0000313|EMBL:KYC36221.1, ECO:0000313|Proteomes:UP000076925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7110 {ECO:0000313|EMBL:KYC36221.1,
RC ECO:0000313|Proteomes:UP000076925};
RX PubMed=23221676; DOI=10.1093/gbe/evs117;
RA Dagan T., Roettger M., Stucken K., Landan G., Koch R., Major P.,
RA Gould S.B., Goremykin V.V., Rippka R., Tandeau de Marsac N., Gugger M.,
RA Lockhart P.J., Allen J.F., Brune I., Maus I., Puhler A., Martin W.F.;
RT "Genomes of Stigonematalean cyanobacteria (subsection V) and the evolution
RT of oxygenic photosynthesis from prokaryotes to plastids.";
RL Genome Biol. Evol. 5:31-44(2013).
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:KYC36221.1}.
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DR EMBL; ANNX02000047; KYC36221.1; -; Genomic_DNA.
DR RefSeq; WP_017742933.1; NZ_KQ976354.1.
DR AlphaFoldDB; A0A139WUV9; -.
DR STRING; 128403.WA1_41570; -.
DR OrthoDB; 9802627at2; -.
DR Proteomes; UP000076925; Unassembled WGS sequence.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.50.80.20; D-Ala-D-Ala carboxypeptidase C, peptidase S13; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000667; Peptidase_S13.
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:KYC36221.1};
KW Hydrolase {ECO:0000313|EMBL:KYC36221.1};
KW Protease {ECO:0000313|EMBL:KYC36221.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076925}.
SQ SEQUENCE 446 AA; 47961 MW; 790D788B849A3104 CRC64;
MLELFSSGLI SIWLEMAGVQ VKPTDVLDIL AWQSSPGLVL APDPNPSGSA IVQQYLKGLQ
TLKLVTTPEQ TQNQGIWLQS GPILMANHQG TTPLPAASLT KIATSLAALT TLGPNHQFHT
LVSTTGSLQN GVLQGDLIVT GGGDPLFVWE EAIALGNSLN QMGIKRITGN LIINGNFAMN
FQRNPLIAGQ MLRQAINSAT WSRAISFQHS LMAKGTLKPQ VTIAGQVKLL AQDVAFFQNP
QQTLLLRHRS LPLRQIIKEM NVFSNNEMAE MLADAVGGAY VVQSKAARLA RVPQSEIQLI
NGSGLGQENR ISPRAACAML MAIQKEAFAH QLTVADFFPT AGFDNRGTLH SRHLPAATVM
KTGTLRDVSA LAGVVPTRDR GLVWFAIINR GYTVPAFRTG QDQFLQTLVK QLQVAPAIPA
SLTPHTATST LPQFGAANRN EMVYGG
//
