ID A0A2N1F957_9FLAO Unreviewed; 446 AA.
AC A0A2N1F957;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Peptidase M28 {ECO:0000313|EMBL:PKH51457.1};
GN ORFNames=CXF68_12525 {ECO:0000313|EMBL:PKH51457.1};
OS Tenacibaculum sp. Bg11-29.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=2058306 {ECO:0000313|EMBL:PKH51457.1, ECO:0000313|Proteomes:UP000233844};
RN [1] {ECO:0000313|EMBL:PKH51457.1, ECO:0000313|Proteomes:UP000233844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bg11-29 {ECO:0000313|EMBL:PKH51457.1,
RC ECO:0000313|Proteomes:UP000233844};
RA Collins E., Ducluzeau A.-L.;
RT "Pharmacopeia of the Arctic Ocean.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634}.
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:PKH51457.1}.
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DR EMBL; PJBB01000003; PKH51457.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N1F957; -.
DR OrthoDB; 9787436at2; -.
DR Proteomes; UP000233844; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR PANTHER; PTHR12147:SF55; PEPTIDE HYDROLASE; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000233844};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..446
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014715893"
FT DOMAIN 110..312
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 446 AA; 50070 MW; F691753CFE289430 CRC64;
MKKIFFFLCC LLSIAVLQAQ TDTKMYDIIN TISTNRIKAD ITTLVNFGTR HTLSDTLSNT
RGIGAARRWI KYELETISKD CNNCLTVFNQ KDLVKKGANK RITKDVWVVN VVAIQKGTKN
PNNYIIMSGD IDSRITDPNN YTDDAPGAND NASGIAGTIE AARILSKYKF DNSIVYVGLS
GEEQGLFGGK GLANYAKNKN WNIIGVINND MIGNIKGVDG VIDNRTFRIF SEPTPTTETE
QQRKARRFYG GEVDGISRQL ARYVYKTTKT YMPEMNPKMI YRLDRFGRGG HHRPFNDAGF
SGIRIMEAHE NYTQQHQNIR IENGIEYGDR LKFVNFNYVK KLTAVNAINL ASIASAPPSP
KNVAIGGIVE AAAKLKWDKV SNVKGYKIYW RDTTSPTWDN SRYVKNNINE FTLEGIVLDN
YFFGVAAVGE NGHESIVSFP SKIIRK
//
