ID A0A1M3MAM2_9BACT Unreviewed; 949 AA.
AC A0A1M3MAM2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Por secretion system protein {ECO:0000313|EMBL:OJX89770.1};
GN ORFNames=BGP01_06055 {ECO:0000313|EMBL:OJX89770.1};
OS Paludibacter sp. 47-17.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Paludibacteraceae;
OC Paludibacter.
OX NCBI_TaxID=1895899 {ECO:0000313|EMBL:OJX89770.1, ECO:0000313|Proteomes:UP000183960};
RN [1] {ECO:0000313|EMBL:OJX89770.1, ECO:0000313|Proteomes:UP000183960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47-17 {ECO:0000313|EMBL:OJX89770.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose
CC residues in alpha-D-galactosides, including galactose
CC oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22;
CC Evidence={ECO:0000256|ARBA:ARBA00001255};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing branched (1->3)-alpha-D-
CC galactosidic residues, producing free D-galactose.; EC=3.2.1.n1;
CC Evidence={ECO:0000256|ARBA:ARBA00001271};
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:OJX89770.1}.
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DR EMBL; MKVT01000017; OJX89770.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3MAM2; -.
DR STRING; 1895899.BGP01_06055; -.
DR Proteomes; UP000183960; Unassembled WGS sequence.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR006558; LamG-like.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR026444; Secre_tail.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR PANTHER; PTHR42970; PECTATE LYASE C-RELATED; 1.
DR PANTHER; PTHR42970:SF1; PECTATE LYASE C-RELATED; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00560; LamGL; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 4: Predicted;
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..949
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012363785"
FT DOMAIN 442..532
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 673..878
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
SQ SEQUENCE 949 AA; 102720 MW; FB243E412B8D40A0 CRC64;
MRKMLASLLC LALLGSVQAQ LPAFPGAEGF GKYAPGARAS ASPTIYHVTN LNDTGSGSLR
DAVSQPNRIV VFDVSGIIRL NSRLVFASNL YVAGQTAPGD GVSVYGNGVS FSGANNIIVR
YMRFRMGIKG DSGKDAAGVA NGKNMIFDHC SFNWGLDETF SVSWDNKGSE PGDITIQNSI
IGQGIMTHSA GGLIQTNGGV TLYRNFYTDN KTRNPKVKGL NQYVNNVVYN WGSGGCYILG
DTEGSSWADI TDNYFIKGPS TGGTTAFNRS TPTFQVYQSG NKIDYTTDGI LNGRDAIASD
YGTVTLVNDR SAFTGIPQAH KPIEGKMTAE QAYYWILDSV GASLPARDEV DRYLIDELKS
LGTRGALINS EAELGLVNGV GNVFNGPRLP DTDNDGIPDS WETANGLNPN NAADALIKHE
SGYLNIERYI NSITAPQPYV KYPTSFSVSK VDENYVVLRW QNNDPGATAV VVEQSADNKE
FSVIKTLASD SSSATITGLT KASTYYFRIK TQRGALSSLY TPSVKAMTIG ADAPPVACTD
PVPAHEALLS EFLQVTLSWS NPSSAGSMLY YNVYVGTSPE QLAQKTAGST SSSYTLAITP
GVTYYWRVDA MNVLGLQTGD LWSFTTGYRP PKEKVAYFAL DETEGSKAVN EIEGEATAQN
FAPVWQAGKI GNGVLMNATP ANAALVQPHY DAILLDNESF SVEMWFKSAG GSVDWYLIHK
GSHVKNTTTG ATGKWFGIQY NKTGSNDRLT WAYDDDITKT DINATPGSAY FDNKWHHLVA
VRDLEMKQAR IYLDGVLKGT KADATATGIG QTENLVIGNT NNPGAQPTNA FQGMIDEVSI
YKGVLAEDEI KAHYNEGLVS GARSLYYEHV VVSPNPFCDE LTVHTGELKS DYRLTISDLS
GRTVYRQQGN VNGQALIVRE LKNLPSGVYM LNIYSAEVQL RQKIVKYND
//
