ID A0A0N1E0L0_9FLAO Unreviewed; 490 AA.
AC A0A0N1E0L0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Peptidase S13 {ECO:0000313|EMBL:KPH12959.1};
GN ORFNames=AMQ68_10640 {ECO:0000313|EMBL:KPH12959.1};
OS Chryseobacterium sp. ERMR1:04.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1705393 {ECO:0000313|EMBL:KPH12959.1, ECO:0000313|Proteomes:UP000037945};
RN [1] {ECO:0000313|EMBL:KPH12959.1, ECO:0000313|Proteomes:UP000037945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERMR1:04 {ECO:0000313|EMBL:KPH12959.1,
RC ECO:0000313|Proteomes:UP000037945};
RX PubMed=26543128;
RA Kumar R., Singh D., Swarnkar M.K., Singh A.K., Kumar S.;
RT "Genome Assembly of Chryseobacterium polytrichastri ERMR1:04, a
RT Psychrotolerant Bacterium with Cold Active Proteases, Isolated from East
RT Rathong Glacier in India.";
RL Genome Announc. 3:e01305-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000037945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERMR1:04 {ECO:0000313|Proteomes:UP000037945};
RA Swarnkar M.K., Kumar R., Singh A.K., Singh D.;
RT "Genome Sequencing of Chryseobacterium sp. ERMR1:04 isolated from Glacier
RT Moraine Ridge soil.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:KPH12959.1}.
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DR EMBL; LIRF01000005; KPH12959.1; -; Genomic_DNA.
DR RefSeq; WP_054510622.1; NZ_LIRF01000005.1.
DR AlphaFoldDB; A0A0N1E0L0; -.
DR STRING; 1705393.AMQ68_10640; -.
DR PATRIC; fig|1705393.3.peg.2264; -.
DR OrthoDB; 9802627at2; -.
DR Proteomes; UP000037945; 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 NCBIfam; TIGR00666; PBP4; 1.
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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..490
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005869971"
SQ SEQUENCE 490 AA; 53624 MW; 20C5071F416A0F35 CRC64;
MVNFRKYVSS VAVLASGLFL AQSTVSTVLY SQAYDNQRSN LNLPSPIAAV VEKTVLSAKE
LVDINVNTMM ADPVLKNATW GFVVYDPKTK KIISSYNENT PLVPASTTKL LTTETALNLL
GENYRWMTQL EYSGSVDENG VLNGNLYVIG SGDPSLGTNK AGAWSYRDIV SDFISGMSRE
GIKKVNGDII IQTALFKGNI SRLPENVVWL ENNNYYLPVG TTREINPANE KLIVKKGNTF
SGEKKFFYVS PYNSQMVFAD KYEGDGVLTT KLPDAPAFLA NTLRATMVKS GLSVTGKVMP
KMTDATPESR KLVSSYKSPT LGDIIYYTNQ HSDNSLAEAL LKTVGFQSKG DQTSESGRIV
VTNHLKEDGF DMLGLNYIDG SGLSRSNNVT PISQVKYLTS LMDEKYYKTY LTSLPIGGQS
GTLKRMFVGT GNGQIFAKTG TLNKVKALAG YMKTNSGKTL VFSLLVNNYS GSVDMVKKRM
EKILEPALDL
//
