ID A0A0R2RZD1_9FLAO Unreviewed; 858 AA.
AC A0A0R2RZD1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Peptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ABR84_03880 {ECO:0000313|EMBL:KRO67868.1};
OS Cryomorphaceae bacterium BACL21 MAG-121220-bin10.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX NCBI_TaxID=1655592 {ECO:0000313|EMBL:KRO67868.1, ECO:0000313|Proteomes:UP000051758};
RN [1] {ECO:0000313|EMBL:KRO67868.1, ECO:0000313|Proteomes:UP000051758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL21 MAG-121220-bin10 {ECO:0000313|EMBL:KRO67868.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase M36 family.
CC {ECO:0000256|ARBA:ARBA00006006}.
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:KRO67868.1}.
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DR EMBL; LICC01000002; KRO67868.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2RZD1; -.
DR STRING; 1655592.ABR84_03880; -.
DR Proteomes; UP000051758; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd09596; M36; 1.
DR CDD; cd04818; PA_subtilisin_1; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR001842; Peptidase_M36.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR026444; Secre_tail.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR NCBIfam; NF038113; T9SSA_dep_M36; 1.
DR PANTHER; PTHR33478; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR PANTHER; PTHR33478:SF1; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF02128; Peptidase_M36; 1.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF52025; PA domain; 1.
PE 3: Inferred from homology;
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..858
FT /note="Peptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006423133"
FT DOMAIN 456..535
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 785..857
FT /note="Secretion system C-terminal sorting"
FT /evidence="ECO:0000259|Pfam:PF18962"
FT REGION 354..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 858 AA; 91902 MW; 51CE675A2ED95AFA CRC64;
MKKLLLLAGF LTFNFGFAQD EARVIREYLG QERAQFNLTA SDVQSPALKS SSFSQSMNVT
TAYANQTHQG IEVFNTTSRF AIRDGQVVSA KLSFASDVAS KINTTAPSIS ARTAILKAAQ
ALGLQAPAQL EELSAEDNTY VFKATDLSLN TIPVALTYQH LSDSQYVLAW DLSLYIMDAT
HYYSVRIDAQ NGALIDTKDW VQHCDFGQGI HEGHAAESIL FAPAKSERAM AMVDAQYRVF
PMPLSNPFDG DDQVVTSPEN LDASPFGWHD TDGVVGAEHT VTRGNNVWAR EDIAGTNNGG
ASPEGGVDLI FDFPYGLPQA PENFTDAATV NLFYWNNIIH DVTYQYGFDE ESGNFQENNY
GNPGNGGDSV NADAQDGSGT NNANFATPPD GGNPRMQMFI WTGSAGPIEL LTINNGPLAG
VYSGVPAGFG GAMPNPALTE DIVLIEDDNS GTSTDTADGC DPIVNGLDLA GKIVVIRRGI
CEFGFKALAA ENEGALAVIM VNNVAGDPIL MGAGAVGAQV TIPLFMVSDV DGEAIIAELL
TGNVINGTID GGATPPSIDG DLDNEIIAHE YGHGVSNRLT GGPVNTSCLG NAEQMGEGWS
DYLGLIMTMQ TGDQASDVRG LAAYASGNPN GIREAPYSTD FSVNDYTYAD TNANVSQPHG
IGFVWASMLW DLTWDLIDLY GFDEDIYNGT AGNNIAFQLV MDGMKLQPCS PGFVDGRDAI
LEADELANNG IHRCLIWEAF ARRGLGFSAD QGNSNSRSDQ TEAFDIPESC NLSTIDSNYD
NNFNIYPNPT RGLIQINSVV DLGATVVSIY DMNGRRVWNN TLELGHHTQI DASALSSGIY
LIKIEGGNYS HTSKLIIR
//