ID   A0A369QQR6_9BACT        Unreviewed;       457 AA.
AC   A0A369QQR6;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Putative zinc metalloprotease {ECO:0000313|EMBL:RDC65636.1};
GN   ORFNames=AHMF7616_04266 {ECO:0000313|EMBL:RDC65636.1};
OS   Adhaeribacter pallidiroseus.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Adhaeribacter.
OX   NCBI_TaxID=2072847 {ECO:0000313|EMBL:RDC65636.1, ECO:0000313|Proteomes:UP000253919};
RN   [1] {ECO:0000313|EMBL:RDC65636.1, ECO:0000313|Proteomes:UP000253919}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMF7616 {ECO:0000313|EMBL:RDC65636.1,
RC   ECO:0000313|Proteomes:UP000253919};
RA   Kang H., Kang J., Cha I., Kim H., Joh K.;
RT   "Adhaeribacter sp. HMF7616 genome sequencing and assembly.";
RL   Submitted (APR-2018) 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:RDC65636.1}.
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DR   EMBL; QASA01000001; RDC65636.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369QQR6; -.
DR   OrthoDB; 9787436at2; -.
DR   Proteomes; UP000253919; 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:UniProtKB-KW.
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.
DR   PROSITE; PS50853; FN3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:RDC65636.1};
KW   Metalloprotease {ECO:0000313|EMBL:RDC65636.1};
KW   Protease {ECO:0000313|EMBL:RDC65636.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253919};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..457
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017019126"
FT   DOMAIN          371..457
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
SQ   SEQUENCE   457 AA;  50816 MW;  5A5BCF2A3C5C3FAB CRC64;
     MKPNSFILSC LTIAFTVAAA PIFSFAQTII KSDPVINQMV QEVSAQNLEN TVRKLVSFET
     RHSLSSTTDK KRGIGAARNW VESEFQKAAA ASNGRLTVTQ DKYVIKADGR RIPVDVEMAN
     VMATLKGTDP TDNRVFIVSG HIDSRNTDVM DVKGKAPGAN DDGSGVAAVV ELARVMATRS
     FPATIIFVAV QGEEQGLYGA KHLADRAKKE NWNLVAMLNN DMIGNSLSDE TNLRDNTHVR
     IFSEGVPALE TEEMAALRKS IGGENDSRSR QLARYLKEMS ERYVPQLEVV LNYRTDRFLR
     GGDHTPFSQA GFTAVRICEM NENYQHQHQN VRTKNNIAYG DFPEHIDYDY LRKNTALNLA
     TLASLAAAPA SPENVGVVTS NLTNQTELRW QTPTTGKKPN GYYILMRETA MPMWQKKIYV
     NDTKALLPYS KDNYFFAVQA VDSEGHESLP VMPKPIR
//