ID   A0A023BW07_9FLAO        Unreviewed;      1089 AA.
AC   A0A023BW07;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=MAM domain-containing protein {ECO:0000259|PROSITE:PS50060};
GN   ORFNames=ATO12_15055 {ECO:0000313|EMBL:EZH74186.1};
OS   Aquimarina atlantica.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Aquimarina.
OX   NCBI_TaxID=1317122 {ECO:0000313|EMBL:EZH74186.1, ECO:0000313|Proteomes:UP000023541};
RN   [1] {ECO:0000313|EMBL:EZH74186.1, ECO:0000313|Proteomes:UP000023541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22II-S11-z7 {ECO:0000313|EMBL:EZH74186.1,
RC   ECO:0000313|Proteomes:UP000023541};
RA   Lai Q.;
RT   "Aquimarina sp. 22II-S11-z7 Genome Sequencing.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the peptidase M36 family.
CC       {ECO:0000256|ARBA:ARBA00006006}.
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:EZH74186.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AQRA01000004; EZH74186.1; -; Genomic_DNA.
DR   RefSeq; WP_051575745.1; NZ_AQRA01000004.1.
DR   AlphaFoldDB; A0A023BW07; -.
DR   STRING; 1317122.ATO12_15055; -.
DR   eggNOG; COG2931; Bacteria.
DR   eggNOG; COG4733; Bacteria.
DR   OrthoDB; 5377264at2; -.
DR   Proteomes; UP000023541; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:UniProt.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR   CDD; cd09596; M36; 1.
DR   CDD; cd06263; MAM; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 3.10.170.10; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR011096; FTP_domain.
DR   InterPro; IPR000998; MAM_dom.
DR   InterPro; IPR001842; Peptidase_M36.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   InterPro; IPR026444; Secre_tail.
DR   NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR   PANTHER; PTHR33478; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR   PANTHER; PTHR33478:SF1; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR   Pfam; PF07504; FTP; 1.
DR   Pfam; PF00629; MAM; 1.
DR   Pfam; PF02128; Peptidase_M36; 1.
DR   Pfam; PF18962; Por_Secre_tail; 1.
DR   SMART; SM00137; MAM; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS50060; MAM_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000023541};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1089
FT                   /note="MAM domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001511947"
FT   DOMAIN          663..836
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   REGION          622..652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          678..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        623..641
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1089 AA;  117775 MW;  3F079B996BD76C72 CRC64;
     MKKGYSFVIL LLLIGQTILA QNSNTLVRNH FRDIAKEASS KTFNTDFSEW RITDEVPSLK
     AGITHVYVNQ LYNGIPIVDG AYKLTVNNGK ITYEIDQFIK EVKSKVTSTK ASSTEISAIN
     AVIRAHNLPP AKRLSKTVSK SNGNDVSQFL DSGITADNEP IKVKKVYKLH NNELRLCWNV
     NLYEKNGHNW WSSYVDTKTG EIIYEDNWVV KCSFEDPDHT SHSHESVLFE TKPLVTVAEA
     PTTALAPDSY NVLAMPVESP IHGSRSIVTN PANATASPYG WHDTNGSNGA EYTITRGNNV
     WAQDDINGNN GTGSSPNGGS SLDFDFPLNL NQDPSNYRDA AITNLFYWNN IIHDVFYQYG
     FNEASGNFQE NNYGKGGAGS DSVNADAQDG SVTCNDPRTN CINNANFGTP PDGSNPRMQM
     FLWNKTNPKR DGDFDNGIIA HEYGHGISTR LVGGPSSNVL GGSEQMGEGW SDFFGLILTM
     KAGDVGTDGR GVGTYALGQP TSGNGIRPTR YSTDTSINST DYGDINNLRV PHGVGYAFAT
     ILWDMTWALI DQEGFDADFY NGTGGNNIAM ALVIEGLKNT ANNPGFVSGR DGILQADKDL
     YNEKYKCLIW KAFAARGVGK DANENNNGGS NTNSDQTVSF VNPCDDPGPD PGNCSGDVTS
     FPFSESFETN LGQWAQATSG DDLNWTRNSG TTPSTGTGPS SAADGTFYLY VEASGNGTGY
     PNKRAILNSP CLNFSSLTTP KLAFQYHMVG SAINTLVVEA RTDNTGNWTS VFSKTGAQGS
     SWNTADVDLS AYAGNASVQL RFNVVTGSGS SGWQSDIAID AVSIQNGTTN PPVCDALNFN
     DFQINAFSNQ DSAGDFSIVS GGAGLSMQNN TWKYISLNYT VTANTVIEFD FSSTSQGEIH
     AVGFENDNSL TSSRYFKVHG TQNYGVTNFD NYASGTKKYV IPVGDFYTGS MDRLVFINDN
     DAGSGNNSIF SNVKIYEGSC GGSLAAETLA AFGSMTPILG DEDEGEVSTI RIAPNPLKKG
     NLLRVFVPSK EISNTSYSII NIMGQVVGEG RLNNNGFINL DRLGAGMYIL KIQNSERKEK
     DTIKRFIIE
//