ID F6GIA8_LACS5 Unreviewed; 943 AA.
AC F6GIA8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Peptidase M16 domain protein {ECO:0000313|EMBL:AEH02294.1};
GN OrderedLocusNames=Lacal_2452 {ECO:0000313|EMBL:AEH02294.1};
OS Lacinutrix sp. (strain 5H-3-7-4).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lacinutrix.
OX NCBI_TaxID=983544 {ECO:0000313|EMBL:AEH02294.1, ECO:0000313|Proteomes:UP000008297};
RN [1] {ECO:0000313|EMBL:AEH02294.1, ECO:0000313|Proteomes:UP000008297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5H-3-7-4 {ECO:0000313|EMBL:AEH02294.1,
RC ECO:0000313|Proteomes:UP000008297};
RX PubMed=21725025; DOI=10.1128/JB.05518-11;
RA Klippel B., Lochner A., Bruce D.C., Walston Davenport K., Detter C.,
RA Goodwin L.A., Han J., Han S., Hauser L., Land M.L., Nolan M.,
RA Ovchinnikova G., Pennacchio L., Pitluck S., Tapia R., Woyke T.,
RA Wiebusch S., Basner A., Abe F., Horikoshi K., Keller M., Antranikian G.;
RT "Complete genome sequences of Krokinobacter sp. strain 4H-3-7-5 and
RT Lacinutrix sp. strain 5H-3-7-4, polysaccharide-degrading members of the
RT family Flavobacteriaceae.";
RL J. Bacteriol. 193:4545-4546(2011).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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DR EMBL; CP002825; AEH02294.1; -; Genomic_DNA.
DR RefSeq; WP_013871073.1; NC_015638.1.
DR AlphaFoldDB; F6GIA8; -.
DR STRING; 983544.Lacal_2452; -.
DR KEGG; lan:Lacal_2452; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_007487_0_1_10; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000008297; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF35; NON-CATALYTIC MEMBER OF PEPTIDASE SUBFAMILY M16B-RELATED; 1.
DR Pfam; PF00675; Peptidase_M16; 2.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000008297};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 49..166
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 206..384
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 531..651
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 678..851
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 943 AA; 105318 MW; 045B3827D71C285A CRC64;
MRILKTTALV AASLLMINCS DSKEEKNTTS ATEFKIDYEK FTLDNGLEVI LHEDHSDPIV
AVATMMHVGS NREKPGRTGF AHFFEHMSFN DSENVPVGAN RKMIPEWGGS RNGGTSNDYT
VYYEVVPKDA FEKILWIDSD RFGYMINTVT KEALEREKQV VKNEKRQRVD NAAYGYTDEI
KRKNLYPENH PYNWTVIGAL PDLQAATIDD VKEFYKKYYG ASNASLVIAG DINIEETKKL
VEKWFGEIPS GPKVESLQPM PVTLEKTKSL YFEDGFAKLP ELRITFPTVE QYNKDKYALE
ILGQVLSGSK KAPLYKTIVE EQKLAPRVGT YQSSSELAGE FVFRVRANAG TDLDNVKSAI
DEGLLRFEKE GVNEKDLKRI KAELETSLYR GVSTVLNKAF QLVEDNEFKG DPSYITQTAK
LTNAVTAEDV MAAYNKYLKG KNYVMTSVVP KGNLDLAVEN AEQATVWIEE VKKDVANEEV
SQGAEAVYEK TPSKHDRSEP GYGELPLFKS PEVWTNELSN GMAIYGIENN EVPLVQFDIT
IPGGHLLDPV EKSGVANLLT DMLMEGTATK TPADLEEAIG LLGASIGMYS TNEDFHITGS
CLAKNFDETI ALVKEIILQP RWDEKEFSRL KKALETSLKG REANPNSIAT LAYNKLLYGD
NHIFAVPGSG TSESTQEITL DDLKKYYKKL SPKEATFHIA GALAASQVKS TLETLNDWNT
KSVEIPTYAI PEANAKNQLY FIDFPGAKQS VIRIGKLALS QENEEANNLR FANEIIGGGS
SGKLFQTLRI GKGYTYGAYS GISSNKEVSP FTVRTSVRAN ATLKSLEIIK NMISNYSSDF
SNNEVELTKN KILKGNTRAY ESLGAQLGML RNISKFNLSH TFTEEDQEEL VNMTLEDYKT
IIDKYLTEED MIYVVVGDKE TQFEEVKKLG KNIIELDING NKI
//