ID A0A162XPT4_9FLAO Unreviewed; 1078 AA.
AC A0A162XPT4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=MAM domain-containing protein {ECO:0000259|PROSITE:PS50060};
GN ORFNames=AWE51_14160 {ECO:0000313|EMBL:KZS38728.1};
OS Aquimarina aggregata.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aquimarina.
OX NCBI_TaxID=1642818 {ECO:0000313|EMBL:KZS38728.1, ECO:0000313|Proteomes:UP000076715};
RN [1] {ECO:0000313|EMBL:KZS38728.1, ECO:0000313|Proteomes:UP000076715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RZW4-3-2 {ECO:0000313|EMBL:KZS38728.1,
RC ECO:0000313|Proteomes:UP000076715};
RA Wang Y.;
RT "The draft genome sequence of Aquimarina sp. RZW4-3-2.";
RL Submitted (JAN-2016) 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:KZS38728.1}.
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DR EMBL; LQRT01000046; KZS38728.1; -; Genomic_DNA.
DR RefSeq; WP_066318394.1; NZ_LQRT01000046.1.
DR AlphaFoldDB; A0A162XPT4; -.
DR STRING; 1642818.AWE51_14160; -.
DR OrthoDB; 5377264at2; -.
DR Proteomes; UP000076715; 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:UP000076715};
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..1078
FT /note="MAM domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007841064"
FT DOMAIN 660..834
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT REGION 376..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1078 AA; 114912 MW; 6337E0072C053944 CRC64;
MKKVYSFAVL ILLIGQTLFA QQDIETAVLN HFKAEAAAAN DAKSSTTNDY SEFKITSTAS
SLKPGLVHAY ITQYLNGTPI VNGTYKVSVE NGQVTYAINQ FVQDAASKVV AAKSSSTPEA
AIGVVARMHN LAQPKSLSKA VIQKNGNDVF EFKNSGITED EKAITAKQVY VYHNNELRLA
WNVNLYEKGG ENWWDSYVDI STNEILHENN WVISCNFDAP GHESHDHNES VLIDANKIGP
LTKAATAALA PDSYNVYAMP LGSPDEGNRS IVTDPANTTA SPFGWHDTNG SAGAEFTITR
GNNVWAQDDS NGNNGTGFSP SGGSSLDFSF PVNLNQAPSN YRDASITNLF YWNNIMHDVW
YQYGFDEASG NFQENNYGNG GSGSDSVNAD AQDGSGTNNA NFGTPPDGSN PRMQMFLWNR
TNPGRDGSFD NIIIAHEYGH GISTRLVGGR NSNTLGGSEQ MGEGWSDWFG LMLTMKAGDR
GTDGRGVGPY VLGQPVDGAG IRPTRYSTNR SINNTDYADI GGLARPHGVG YAFATILWDM
TWALIDQEGF NPDFYNGTGG NNIAMALVIE GLKNTANNPG FVSGRDGILQ ADQDLYNGQY
RCLIWKAFAE RGVGQDANEN NNGGSNGQTD QTVSFVNPCD GGGPGPGGDD CTGDVTSFPF
AESFETNLGL WKDATSGDDL NFTRNSGGTP SNGTGPSSAV DGSTYIYVEA SGNGTGFPNK
RAILNSPCLN FSGLTSPSLT FQYHMVGSAI ESLTVEARTD NTGNWVSVFN RAGAQGTNWN
AADVDLSAYA GNASVQLRFN VLTGDGGQGW QSDIAIDAVS IQDGTGNPDP TCDALSFNDF
TISPFSNQDT ATGNNATVIN GGAGLSMSNN TWKFIALNYT VTANTVIEFD FSSTAQGEIH
AVGFEDDNTL TQTRYFKVHG TQSYGVLDFD NYAGGTTTYT IPVGNFYTGS MDRLVFINDN
DAGSGNTSVF SNVKIYEGSC PGSSVVASFG PTTPTLGTEN EGAFAMRVHP NPLSKGSSLQ
VSISGKQLSE TPYSIINIMG QVVGKGKLNN SGSINVSRLG AGMYILKVQD STQRFIIQ
//
