ID   A0A1H9AHV7_9FLAO        Unreviewed;      1875 AA.
AC   A0A1H9AHV7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Por secretion system C-terminal sorting domain-containing protein {ECO:0000313|EMBL:SEP76067.1};
GN   ORFNames=SAMN05421824_0242 {ECO:0000313|EMBL:SEP76067.1};
OS   Hyunsoonleella jejuensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=419940 {ECO:0000313|EMBL:SEP76067.1, ECO:0000313|Proteomes:UP000198999};
RN   [1] {ECO:0000313|EMBL:SEP76067.1, ECO:0000313|Proteomes:UP000198999}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21035 {ECO:0000313|EMBL:SEP76067.1,
RC   ECO:0000313|Proteomes:UP000198999};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
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DR   EMBL; FOFN01000001; SEP76067.1; -; Genomic_DNA.
DR   STRING; 419940.SAMN05421824_0242; -.
DR   Proteomes; UP000198999; 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; 1.
DR   CDD; cd03859; M14_CPT; 1.
DR   CDD; cd06263; MAM; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 6.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR033810; Carboxypeptidase_T.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR032179; Cry22Aa_Ig-like.
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; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR   PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR   Pfam; PF16403; Bact_surface_Ig-like; 5.
DR   Pfam; PF20009; GEVED; 1.
DR   Pfam; PF00629; MAM; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   Pfam; PF18962; Por_Secre_tail; 1.
DR   SMART; SM00137; MAM; 1.
DR   SMART; SM00631; Zn_pept; 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; 1.
DR   PROSITE; PS50060; MAM_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000198999};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          801..887
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1130..1288
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
SQ   SEQUENCE   1875 AA;  201916 MW;  C19F5E8F4B116C23 CRC64;
     MKKIAFTLVV VFNVLFTFSQ QNQSPKRISI ANPSQNTLQK IQKAGIDLSC GPRFINNNLE
     MELGYEELQA LKKNGISYQV LINNLTKYYS DRNTFDLPIA KNELRSLKKK PKKQFDGSTS
     TQKSLSLQNI LVGNPTQHDE CSEINWPVPS NFQLGSMGGC LTVSEALAQL DLMRSLYPNI
     ISVKTDASPT GQTTHGNSTG STTWPGQTVY YVRISDNPDI DEPSEPETLI TGMTHSREVN
     SLMNVMYFMW YILENYNSDP FIKNVVDNQE LYFIPIVNPD GLRWNEVIAP NGGGLQRKNL
     RPGVADNGST GTSNNVRGVD LNRNFNYYWG WDDAGSSPTS SSNTYRGPSA GSEPETQILQ
     DFVLNHDIKV AVNHHGGLNS IVTSSYNGSV SAADSGREDE YAKICHDLTH YNRYIYGSAP
     NTLYEANGDT NDWMLGGSPV SSGGQTSSGS GKDVLAFAPE NGDDFWPAPS QITPIAQRAL
     RMNFLSVLYS GKFAKLHDLN LSTISSTSGN LTFGVEYLGK TYDDITLSVT PVSSNITSIS
     SPSTQSGWTK LEQRNLSVPY TLDPGILPND EIEFQVTLSN NEFVLYQANY VKYYQANVLF
     SDNPDVTGTS NWTTSGGSWG TTSDAYSGST AITDSPSGSY NNNENKSITL NSTIDLSGTS
     QVLVQYYAKW DLERNYDLVQ IEASTNSGGS WTALCGNYNK PAAGFDTNFH LNKNTSTFRN
     HQSANGDIIY DGDTMDKWVM EEIYINATEN TFLLGQNNVQ FRFRLKSDSL NREDDLTTTF
     DGFIFDDFKI ISIQTPCVLS VPAAVAINSI AEASAAISWD LIPSATYDLR YREVGSQNWT
     DVNGLSTPNY DITGLTNVTD YEVQVRSNCS TNSSAYSSVI TFTTLDVQLN YCASASTNVN
     DEFISRVQLN TINNTSGAQF YSDFTNISTS LEKGTQYTIT ITPTWTGQVY TEAYSVWIDY
     NRDGDFEDAG EQVFTQSPTN ASSVSGSFTV PASAVENSTR MRVSMQYNAI PTSCQTFQFG
     EVEDYTIIVE GAGPDVTPPV ITLNGASPVS VTIGGTYSEE GATATDNIDG DISANIVVGG
     DTIDVNTLGS YTITYDVSDA AGNAATQVTR TVNVVEAVPG CSGGIAVFPY TQGFEGSIGD
     WSQSSADDLD WLVNSNNTPS NNTGPSGAVQ GSSYIYVEAS GNNTGYPNKR AIINSPCFDL
     SNATGADFSF QYHMFGAADM GTIDLEISND DGASWISIWN QSGNQGNSWF VVNLDLSTYA
     GGSIQLRFNR FVGSTWQADI AIDDINLTTI EEDTIAPVIT LIGASSIDLD VGGTYNEQGA
     TATDNIDGDI SASIVIGGDV VDTNIAGTYM VTYNVSDAAG NAATQVTRTV NVIPDTTAPV
     ITLIGASSID LDVGGTYNEQ GATASDNIDG NISASIVIGG DVVDTNIAGT YVVTYNVSDA
     AGNAATQVTR TVNVIPDTTA PVITLIGASS IDLDVGGTYT EQGATATDNI DGDISASIVI
     GGDVVDTNIA GTFIVTYNVS DAAGNAATQV TRTVNVIPDT TAPVIALIGA SSIDLNVGGT
     YTEQGATATD NIDGDISASI VIGGDVVDTN IAGTYMVTYN VSDAAGNAAT QVARTINVNA
     IPTDVVLHQG FFETGLDGWT DGGSDCARRQ DTRSYEGIYS VRIRDNSGTA SAMTYSNVDI
     TGFAEVQVNF YFYVVSMENN EDFWLRYYNG SSWTTIETWA RGIDINNDTF YNATVVIPAS
     VYNFASNSGF RFQCDASGNN DQIFIDQVTI TGLSSASGSN NTLTNLGGTT KTGTDKYFDE
     EEEFIVYPNP VKGIELNVFV PGTDIFDFKI INMLGQIVAE GKSEGKIMVD RIESGVYIIE
     VNDGDELMTK RFIKE
//