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Database: UniProt
Entry: A0A1Q7UQK6_9CHLR
LinkDB: A0A1Q7UQK6_9CHLR
Original site: A0A1Q7UQK6_9CHLR 
ID   A0A1Q7UQK6_9CHLR        Unreviewed;       241 AA.
AC   A0A1Q7UQK6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Peptidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AUG82_05765 {ECO:0000313|EMBL:OLE04624.1};
OS   Ktedonobacter sp. 13_1_20CM_4_53_11.
OC   Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC   Ktedonobacteraceae; Ktedonobacter.
OX   NCBI_TaxID=1805225 {ECO:0000313|EMBL:OLE04624.1, ECO:0000313|Proteomes:UP000186213};
RN   [1] {ECO:0000313|EMBL:OLE04624.1, ECO:0000313|Proteomes:UP000186213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
CC   -!- SIMILARITY: Belongs to the peptidase S51 family.
CC       {ECO:0000256|ARBA:ARBA00006534}.
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:OLE04624.1}.
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DR   EMBL; MNIY01000112; OLE04624.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7UQK6; -.
DR   STRING; 1805225.AUG82_05765; -.
DR   Proteomes; UP000186213; Unassembled WGS sequence.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd03129; GAT1_Peptidase_E_like; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR005320; Peptidase_S51.
DR   PANTHER; PTHR36175; CYANOPHYCINASE; 1.
DR   PANTHER; PTHR36175:SF1; CYANOPHYCINASE; 1.
DR   Pfam; PF03575; Peptidase_S51; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825}.
SQ   SEQUENCE   241 AA;  25052 MW;  989D51B6A1BA9E88 CRC64;
     MGVPTPGTLA LVGAGEFLPP IAPVDAMLLE RVDGTPHVVV LPTASAPDGP GVPERWAKLG
     IDHFSQLGAS AEAVMLLERG DADDDSIVAR VAAANFVYFS GGKPRYLLET LKDTAAWQAI
     MRVLAAGGIL AGCSAGAMVL GGELFDFPQL WRTIPALGIA PGIIVIPHFD EIPAAFTSTM
     TLAKRKLTLV GIDGSTALVR SDGAWSVYGR GGATVFNGNH KRRFASGEQV PLPGEANRAG
     K
//
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