ID A0A2M9C8L1_9FLAO Unreviewed; 998 AA.
AC A0A2M9C8L1;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Putative secreted protein (Por secretion system target) {ECO:0000313|EMBL:PJJ67180.1};
GN ORFNames=CLV73_1182 {ECO:0000313|EMBL:PJJ67180.1};
OS Chryseobacterium geocarposphaerae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1416776 {ECO:0000313|EMBL:PJJ67180.1, ECO:0000313|Proteomes:UP000228740};
RN [1] {ECO:0000313|EMBL:PJJ67180.1, ECO:0000313|Proteomes:UP000228740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27617 {ECO:0000313|EMBL:PJJ67180.1,
RC ECO:0000313|Proteomes:UP000228740};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): From Individual Species to Whole Genera.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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:PJJ67180.1}.
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DR EMBL; PGFD01000001; PJJ67180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9C8L1; -.
DR OrthoDB; 8737820at2; -.
DR Proteomes; UP000228740; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:UniProt.
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; 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; PF00041; fn3; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR SMART; SM00060; FN3; 2.
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; 2.
PE 4: Predicted;
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..998
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014896280"
FT DOMAIN 473..568
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 571..670
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 560..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 998 AA; 107373 MW; 9FC4856A553BCA6B CRC64;
MKKPLLTKQT LTALLFCGLT FSTLDLNAQT LAFPEATGFG RFTTGARGAA NPQIYLVTNL
NDSGPGSFRD AVSQPGRFVI FRVGGIVNLQ SVVAVAANTT IAGQTAPGEG IVFLGPRVSF
TGANNTIARY LRLRYGGTAQ NQDASGIANG ANIILDHMTF TWGTDEVFSV NWDGNGTSPD
NITIQNSIIG QGMHRHNHSA GGLMQPPPGG KISLIGNLYI CNKTRNNKIK GINEFVNNVV
YNWGNYGNIY GHTQSGEAYI MGGDSAGPSY ANIINNYFIG GPNTSTTVTT PFSVGNANFN
LYGSGNYFDN NRNGVLDGTL VPQNLTGYPV GDVAAIQTAP YDYPMKNTTV TAQTAYDNII
AGAGASYPRR DQVDQLMISD LMSKGTTATY VYVQTDLTTQ FGFTNGGAGH VYGAPAPLDT
DNDGMPDAWE IVNGLNPNVF DALAVSTTHA PYLNIEVYIN GLHNTPAPDF IIPPTNLNFT
NAVTAGTPAS SSLTVNWSDN ATNETNYVLE RSNDGTNFTV IATLPANTVS YNESGLTPNT
QYYYRVKAIN ATESSVYTSS ASVTTPPVPS APTKPTSPNP TNGNNYVELS SGNLLLKWNG
SSNTTTYSVY FGTNPQSLSN IGTVAYSATP SYQLTNLNTG TDYYWRIDAS NALGSVTGDV
WSFRALTPSL VGNWPFSEAP LSGEQITDIS NYANHGTLNV AYDNSNVRVP GKENFALDLA
TAPNTYIASI PHQDQIFFNN NSFTVSFWMK APTTMIPSSS STSLYVLCKG SFTKNTTTGA
TGKRFNVEIK GGQLRYAIDD DITKKEITSP IANYFTGNWV HVVIMRDIAA HKMRIYTNGV
LSAEGDETAV TGIGETSDFI IGNIGELEFL STANAPAPYK GAFDELKMYN YALSPSEITA
LYNQNVLQND EFSISKNVGT VYPNPVKDQI FINLPEYKRS DLTATLIDMT GKVVIKEKIK
SGKDGVFNLN ISYIKAFGNY ILNVSGENLN SNFKVVVK
//