ID A0A0R0CU44_9GAMM Unreviewed; 661 AA.
AC A0A0R0CU44;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Peptidase M20 {ECO:0000313|EMBL:KRG72832.1};
GN ORFNames=ABB28_13680 {ECO:0000313|EMBL:KRG72832.1};
OS Stenotrophomonas chelatiphaga.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=517011 {ECO:0000313|EMBL:KRG72832.1, ECO:0000313|Proteomes:UP000051386};
RN [1] {ECO:0000313|EMBL:KRG72832.1, ECO:0000313|Proteomes:UP000051386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21508 {ECO:0000313|EMBL:KRG72832.1,
RC ECO:0000313|Proteomes:UP000051386};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KRG72832.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LDJK01000064; KRG72832.1; -; Genomic_DNA.
DR RefSeq; WP_057509141.1; NZ_LDJK01000064.1.
DR AlphaFoldDB; A0A0R0CU44; -.
DR PATRIC; fig|517011.3.peg.2657; -.
DR Proteomes; UP000051386; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd06461; M2_ACE; 1.
DR Gene3D; 1.10.1370.30; -; 1.
DR InterPro; IPR001548; Peptidase_M2.
DR PANTHER; PTHR10514; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR PANTHER; PTHR10514:SF27; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR Pfam; PF01401; Peptidase_M2; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000051386};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..661
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006394677"
SQ SEQUENCE 661 AA; 73447 MW; EB2D391EBD5C9D6A CRC64;
MKHRHLLLAS AIAAATLSLA ACKKEPTPGT DTATAMAPAG ETADQFVARI NAEYKAAYPE
MTSAQWLSST YINGDSERVA AKANERSLTQ LNSWIEQAAK FEGQPMSDDS KRALRLLKLM
SSMPAPRDPA KLAQLTQIAT RMEGSYGAGK YCTDANDPNS CRQLGDLEQV LSSSRDYDQQ
LDAWQGWHGT TRNMRGDYQQ FVGLVNEGAK GLGFADAGQM WRSGYDMPPE QIGPETDRLW
EQVKPMYEQL HCYARGKLDA TYGKDKAEVG NGLIAAHLTG NMWQQDWSNL WDQLQPYPGA
GSLDITAALE KQYQGNLSGA LAKAGSNANV ESLYKAQREA ELRTARQMTE RAQDFYVSLG
MPALPKSYWE NTQFIKPQDR DVVCHASAWD MNMEGDVRTK MCIKPNEENF TTIYHELGHI
YYDLAYNPLP PLFQGGANDG FHEAIGDTIV LAMTPKYLNS IGLVDKPEES REAVINNQMR
MALSGVAFLP FGLMIDRWRW GVFDGSITPD NYNKAWWDLK ARYQGVAPPT TRGEEFFDPG
AKYHVPGNTP YTRYFLARIL QFQFYKGLCD ASGYKGPLHE CSFYGNKEAG QKFWSMLSKG
ASQPWQATLK ELTGGDKLDA GPMIEYFTPV NAWLKEQNQG QVCGWQASAA APAAPAAPAQ
R
//