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Database: UniProt
Entry: A0A1J5IAF6_9GAMM
LinkDB: A0A1J5IAF6_9GAMM
Original site: A0A1J5IAF6_9GAMM 
ID   A0A1J5IAF6_9GAMM        Unreviewed;       427 AA.
AC   A0A1J5IAF6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Peptidase S13 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AUK56_09835 {ECO:0000313|EMBL:OIP94213.1};
OS   Thiomicrospira sp. CG2_30_44_34.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Thiomicrospira.
OX   NCBI_TaxID=1805397 {ECO:0000313|EMBL:OIP94213.1, ECO:0000313|Proteomes:UP000182935};
RN   [1] {ECO:0000313|EMBL:OIP94213.1, ECO:0000313|Proteomes:UP000182935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG2_30_44_34 {ECO:0000313|EMBL:OIP94213.1};
RX   PubMed=27112493;
RA   Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA   Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT   "Genomic resolution of a cold subsurface aquifer community provides
RT   metabolic insights for novel microbes adapted to high CO concentrations.";
RL   Environ. Microbiol. 0:0-0(2016).
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:OIP94213.1}.
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DR   EMBL; MNZS01000065; OIP94213.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J5IAF6; -.
DR   STRING; 1805397.AUK56_09835; -.
DR   Proteomes; UP000182935; 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; 2.
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; 1.
DR   PRINTS; PR00922; DADACBPTASE3.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..427
FT                   /note="Peptidase S13"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012046272"
SQ   SEQUENCE   427 AA;  47765 MW;  0EE3046FBC33580C CRC64;
     MQNKIQNRVR FFLRVWLFMS LSMVLQAQPV PSIFAELDNA SLFLLNAQHQ VVMAKHADKA
     MIPASTTKLM TAFLALQHWG AEHRFHTNFY LSHTANHEAV LMVKGYGDPF LISEEIEHLA
     KTLAQRLKAQ KIESLSHLVL NTDYFQANVI LPGHSSTQNP YDAIPSVLAA NFNTLNVEQQ
     QGILVSAEPQ TPLTPVARAW AMQPEVDLSQ GRVNLGAQAK RCENYFAELL SHFLSKEGIR
     IQGSVVWGSL PADQSHLIYQ HDNSHTLAEL IQPMMRYSTN FIANQLALIL SAERYGAPAT
     AEKVAKMFQE EIIGQFGWQD FKVEDGAGLS RQNRLSAKQL VMLLQKFKPW RHLLPEIMPQ
     VVAKSGTLIG VTTLAGYIEV PISGRAEQLQ WAPFALLINE PASYHTRNQI TQRLKTALAS
     QSLVSAP
//
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