ID A0A1M6AYC4_9FLAO Unreviewed; 1080 AA.
AC A0A1M6AYC4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Por secretion system C-terminal sorting domain-containing protein {ECO:0000313|EMBL:SHI41223.1};
GN ORFNames=SAMN04488508_101529 {ECO:0000313|EMBL:SHI41223.1};
OS Aquimarina spongiae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aquimarina.
OX NCBI_TaxID=570521 {ECO:0000313|EMBL:SHI41223.1, ECO:0000313|Proteomes:UP000184432};
RN [1] {ECO:0000313|Proteomes:UP000184432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22623 {ECO:0000313|Proteomes:UP000184432};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FQYP01000001; SHI41223.1; -; Genomic_DNA.
DR RefSeq; WP_073313532.1; NZ_FQYP01000001.1.
DR AlphaFoldDB; A0A1M6AYC4; -.
DR STRING; 570521.SAMN04488508_101529; -.
DR OrthoDB; 1652165at2; -.
DR Proteomes; UP000184432; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:UniProt.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00063; FN3; 2.
DR CDD; cd18173; M14_CP_bacteria; 1.
DR CDD; cd06263; MAM; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR045474; GEVED.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000998; MAM_dom.
DR InterPro; IPR000834; Peptidase_M14.
DR InterPro; IPR026444; Secre_tail.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR PANTHER; PTHR11532:SF57; PEPTIDASE_M14 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11532; PROTEASE M14 CARBOXYPEPTIDASE; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF20009; GEVED; 1.
DR Pfam; PF00629; MAM; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00137; MAM; 1.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50060; MAM_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000184432};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1080
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012793616"
FT DOMAIN 494..580
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 591..756
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 761..846
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 242..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1080 AA; 117443 MW; 19C6E5A73C721D59 CRC64;
MKKSAILLLM VVFTVSSTLF GQQNEQQLAE TYLNTKGEVI FDFVISNKSE LNTITKELAI
VYYDDLTRTV KVMADADQFA SFLAKKTPFS INPEDNVIGY RTMTSDLTVK AATFPLTAYP
TYADYVSIMN DFATNNPTLC KVENIGATTE GDKSLLFVKL SDNVDSNEQE PRVMYTSSMH
GDEIAGYPMM LNLIDLLLTA YKDTSHPRHA EIKNLLDTSE VWINPLANPD GTFRNSPTNT
SVANATRGNA NNVDLNRNYP DPDDGPNPDG NAYQTETLAF MNLADAKHFV LSANFHGGIE
LVNYPWDTFA GAHPDEDYFV HISEEYRDLC QANSPAGYFD ALNNGITNGY DWYEVQGGRQ
DYQIYFKKGR EVTVELSNAK TPPASQLVNF WNYNEDALIA YLKQVTYGIR GVVTDAITNQ
PVDAKVTVIG KEGFESWVPT ELPEGDYYRP IKAGTYDIKY EADCYEPLTV TGVAIADFAT
VVQDVQLNPI AGQAPDGLQA TSIQTSTATL NWNSSTGATY DVRYREVGTT NWTTVATATN
SLALTNLNAT TAYEAQVRSN CSGGVSSPYS TSVTFTTTDV PTCAGVSVFP YTESFETDLG
VWTNDTGDDI NWTRDSGGTP SQTTGPSSAQ DGNFYLYLEA STNVSPPGSP NKTAILNSPC
IDLSSLSGAT LEFGYHMYGA TMGSLEVLIS NDDGANYTSL WSQNGNLGNS WNQASLDISS
YTGSVVKVQF KGVTGSSWRS DMAIDNIRVI SSTVDTEAPT APTNLVSSNI TSNSVTLSWE
AATDNIGVTA YDVYQGTTLI ATVNGLVHIA SGLTPNTAYS FSVIAKDGAG NSSPSSNVIN
ATTIDGGITY CNSQGNNVNY EYIDLVALNQ INNPTGANGG YADFTSQIAD VPYGSNSITL
SVGFVNTAYT EFWSVWIDYN KDGTFDAAEQ VVSESTNSSA NQTYTFSVPT TALSGNTRMR
VSMKYNSAQG PCETFTYGEV EDYTVNIGGV VSKGNDIAQI PLSNKVNLYP NPIYGNTLHI
GGLKQLNDAN YQIFNYVGQN VLQGRMMEVK QIDVSTLPNG VYVIEISKEK NKWTNRFIKM
//
