ID A0A227P2M8_9FLAO Unreviewed; 2001 AA.
AC A0A227P2M8;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=MAM domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=B0A64_16815 {ECO:0000313|EMBL:OXG03793.1};
OS Flavobacterium araucananum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=946678 {ECO:0000313|EMBL:OXG03793.1, ECO:0000313|Proteomes:UP000214684};
RN [1] {ECO:0000313|EMBL:OXG03793.1, ECO:0000313|Proteomes:UP000214684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24704 {ECO:0000313|EMBL:OXG03793.1,
RC ECO:0000313|Proteomes:UP000214684};
RA Stine C., Li C., Tadesse D.;
RT "Whole genomes of Flavobacteriaceae.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M4 family.
CC {ECO:0000256|ARBA:ARBA00009388}.
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:OXG03793.1}.
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DR EMBL; MUGS01000036; OXG03793.1; -; Genomic_DNA.
DR Proteomes; UP000214684; 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:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09597; M4_TLP; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000998; MAM_dom.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR InterPro; IPR026444; Secre_tail.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR PANTHER; PTHR33794:SF1; BACILLOLYSIN; 1.
DR Pfam; PF00629; MAM; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 269..417
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 420..591
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT DOMAIN 1444..1589
FT /note="MAM"
FT /evidence="ECO:0000259|Pfam:PF00629"
FT DOMAIN 1928..1999
FT /note="Secretion system C-terminal sorting"
FT /evidence="ECO:0000259|Pfam:PF18962"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 410
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 502
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 2001 AA; 222151 MW; B25747E672F3E06B CRC64;
MALEASDTVK EQVSKKESDP DSIKNSATNT LLIQEEENIK GTALSEKENE SIKKQIQESQ
KLLEQKLTNT PERTSAQDSV RTASKSFAKS SNLTAKNIFE VKKGEFDLAK SDQMQLKSIS
DSHGRTLVTY QQLHNAVPVE GAIYKVRENK SKIDAFGFTT QKLPVNSNYK INAATGLENA
LKTVNAKQYI WESKKLGTII NKSISTKPQG ELVYVGPNFS SELKEYYLAW KYDILATNPQ
SSQTIYVDAN SGKIILTIDL NRDAGQSLGK GKSRYSGDVT FNTKQYADGF RLEAIQGKYK
VPMYTLNMNH ADNASDEVIT DFIDEDNIWN DLYNKNNDEV AIDIHWGMQK TIDYYAEKFN
RNSVDNKGMQ IIGLAHLGNN VENASWTGGW AQFGDGKNTP YVGLGITAHE LTHAVTQFSA
GLIYRGESGA LNESFSDMLG VSVEFYVGID KKEDIWMLGN ELYQHGSMRN MSNPKAQGQP
DTYGGKNWAN PSNTNYDNGG VHINSGITNY WFYLLSEGGQ GINDLNSSYD VKAIGIAKAE
KIAYTTLTEY LSPSSNFSDM RLASLMATED LYGLGSEEYK QVTNAWYAVG IGAAFADKQI
SLVSVENAAT ICGPLKGDEP FYIKIKNTGS SVIKANDILN YKLRLMISSF GSKYTSLYTN
DGTTGFTKEL GVGEETIIKV QDQLPYEISA TTINYVEIKL DFKPIAEFGT KEGVSFVSSL
LNPPAQKDFD IKLIGLNLPE YSGEALSANY PLAIKIYNLG CQDIPAGSQL KVGYLNKLPG
NETVWKDVTL STAFKMNSEM TIPFDGTVDL SAVGVHTYEA FVTYSPDPVT ANNSGIYAVY
NGVVTQFPYY QDFEGTPGGW YSKSILTNQK FVWQATSYSF RDTNSKYLWG TVTLGTSEKL
PLNADFTLQS PIFDFTNVAS PYVEFDMIYL FIRGYHGLVV EYSEDNQNWQ KVTGIDYPNT
EHYNNLISGP WFSGINNNSD KPPIAMRLNE LAGKKAAIRF RVVTDNNSTT YLGAFIDNIR
VSDAPYDLEV IAAEADAGTC TINNDNVTIK TRIINNFNTS SEQVNVTVKI LDSEKNEIFS
KNENTTLLFT KYRDTITYSI SNINLKSIGK NTISVSVFPL DMAKDVKPEN NSLSFGSDNW
NNEDMKVTVL PYTMDFEEVT KYKGWRTTEN KNSAGWKHGL RADLDSPGWS VDDHTHFMAS
NDDKCNCDSS NDMLISPVFD LSNYKEARLT FDGFGDGARL SDGYVKVSTD GGETWKTIFK
MPYISNWINY HVDLSPYAGN PCVLIAFQHD DNGLFASGFA VDNIKIQDTT EYLELSNLSV
AENVYEDAPM HQFFVSAKNV SYNTINKVTI EYQITQNGVA VGEPIVLERT NQLLQYQTSV
YNIDGIPQLA AGNYEINIKL MAEGQPKALA ESLTGTFKVL AKAPQLNLES FSNVPQGSLF
GEKGFVSNQS DQNYPWRAVV TPDNANPPLP KKDHTGDASA IMLYSQLEYS AVYSEVISPL
YKLAENANAL EFYYALNSNY SNAFIVDLKT TGGEWTEAWR VTTQESYINK EWQKGVINLG
KYAGKSVMLR FRHAKAGGYS YMVLDDLKVI TDPILDVSVQ ILSPKDVCGG SQVKVKLTNE
GQILIKQKTI QLDLEYTNTA ETISEIVPVE IPAGESIEYI FRKQPVLDTS GDSHVFNVMA
KLENDLIPEN NQIKNYVYQE VSSDFKIFDT PVIHGYAGKN LYINAETNFS AKKLEVVSYK
WNTGDVSNGI EINKAGDYLV TVVMKNGCIL TETITATFDT FESELVSGDT CGPQVVLSPG
DYQSYEWLDG STEPTYVTTE SGNYYVTVYN QNGIGKTFST TVSILENSIV PEIQVAGNKK
LTASVEAASY QWFLNDRPIP NATQKSIITF WEGNYRLQIT NNSGCSTVSA PFDSKGMLLG
KITNPFRVFP NPAVDIVNVF LADKTEGATE IKIYAIDGKV VWSKSYTNIP STINVSALSP
GVYILDCSIQ DKKYTARIIK K
//
