ID A0A1M6K6E5_9FLAO Unreviewed; 821 AA.
AC A0A1M6K6E5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Por secretion system C-terminal sorting domain-containing protein {ECO:0000313|EMBL:SHJ54572.1};
GN ORFNames=SAMN04487908_11945 {ECO:0000313|EMBL:SHJ54572.1};
OS Aequorivita viscosa.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aequorivita.
OX NCBI_TaxID=797419 {ECO:0000313|EMBL:SHJ54572.1, ECO:0000313|Proteomes:UP000184172};
RN [1] {ECO:0000313|Proteomes:UP000184172}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26349 {ECO:0000313|Proteomes:UP000184172};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
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DR EMBL; FQYV01000019; SHJ54572.1; -; Genomic_DNA.
DR RefSeq; WP_073219621.1; NZ_FQYV01000019.1.
DR AlphaFoldDB; A0A1M6K6E5; -.
DR STRING; 797419.SAMN05216556_107122; -.
DR OrthoDB; 9792152at2; -.
DR Proteomes; UP000184172; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR CDD; cd04842; Peptidases_S8_Kp43_protease; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR026444; Secre_tail.
DR InterPro; IPR034058; TagA/B/C/D_pept_dom.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000184172};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..821
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009918894"
FT DOMAIN 648..738
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT ACT_SITE 129
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 156
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 339
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 821 AA; 89057 MW; BB0AEDC0AD8796BE CRC64;
MNKPFLLIFY VFFLTANFVN AQTDDQRAQI ISHYDLQKLS ELEQQFDKTF IAERANALRL
AAINGWKETI EQPNGGVAIL VGVFSDGTPK YYQTHNRGAG QTTRADRVHT NGGAELNLNG
ENMIGGVWDG GRTRATHLLL ENRVTQIDNP SSLSSHATHV AGTMIGTGSV IVGIAKGMAP
EAELLAYDFL NDESEMAAAA ATGLLVSNHS YGLRIENLPL WRIGYYDDNA RNLDNIVYNA
PYYLPVCSAG NDRRSGQNSG DGGYDYLTDK SVSKNSIIAA AVYQVTNYSG PSSVVMSSFS
SWGPTDDGRI KPDISGKGVN TYSSTANTNS SYSSYNGTSM SSPSIAGSLL LLQQHYNNIH
GFFMLSSTLR GLALHTADEA GSAPGPDYRF GWGLLNIEKA AEVISNNGNE SIIIEEELAQ
GEVYTFSVQA DGVNDLVASL TWTDPAGRSP QAGINDLDTP MLVNDLDLRI SDDGGITFYP
WKLNPAIPNA AATNGDNTVD NIEKIEIANP SGEYIIRVSH KNVLTNDSQV FSLIVTGINR
EDFAVTTHQG FQDFCPGQIS ATCNIDLDFS DGFSDTIDFS VSNLPSGVEA VLTPDTLNSE
GTVILTLNNI DALAPGDYQV KVTATGATET VNVYPIIHIV DSQLSGVALT SPANGEMNQP
LDMNFTWEDA GMDAEEYDFQ LAMDADFTTV IADVTIEENY TAVDNLLENT EYFWRVRATN
ACGDGEYSDV FNFVTETVVG VDDNMLNELV IYPNPATSVL NIKANSIIDS VEIISVLGKS
VIQTVETDSK AQIDTGNLRA GHYFVRIISE NRVIVKRFIK R
//
