ID A0A0R2FZ49_9LACO Unreviewed; 433 AA.
AC A0A0R2FZ49;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:KRN31525.1};
GN ORFNames=IV36_GL001647 {ECO:0000313|EMBL:KRN31525.1};
OS Liquorilactobacillus mali.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1618 {ECO:0000313|EMBL:KRN31525.1, ECO:0000313|Proteomes:UP000051727};
RN [1] {ECO:0000313|EMBL:KRN31525.1, ECO:0000313|Proteomes:UP000051727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27304 {ECO:0000313|EMBL:KRN31525.1,
RC ECO:0000313|Proteomes:UP000051727};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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:KRN31525.1}.
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DR EMBL; JQAR01000004; KRN31525.1; -; Genomic_DNA.
DR RefSeq; WP_056990677.1; NZ_JQAR01000004.1.
DR AlphaFoldDB; A0A0R2FZ49; -.
DR STRING; 1618.IV36_GL001647; -.
DR PATRIC; fig|1618.3.peg.1673; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000051727; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 63..175
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 181..347
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 433 AA; 49276 MW; 9E5C595FADC38450 CRC64;
MKIIDYPNFE EKVYQEVLPN GLIVNLVPKV GFHKTYASFT VNYGSVDSTF TSLDDNKIMN
RPDGVAHFLE HKLFEKPDYD AFELFGQLGA DSNAFTSYTK TSYLFSTVEN VRKCLDTLLD
FVQFPYFTKE SVEKEKGIIT QEIMMYNDDY NWRLYSGIVE NLYPHSPLSK DIAGTVESIQ
NISSKDLYDC YQTFYQPSNM DLFVVGAINP NEVIRWVEEN QSKKQFPSAP QIMHSKTMIN
DKYDIIPHRT LRVDTSRPKV AVGIRGNIEL PAGKMGLKYK IALNIGMYLL MGESSEAYNK
LYNEGLIDDS FDYDISVGRG YHFCVISGET SNAEKLIMKV MELLKTANEA IGGQRAEFIL
AKKEFIGRQI QSMNSLEGIA NRHEGKLFDG ALSFDAVKIL EELEMKDILQ AVGEFIEPDN
ISVYQVLPKE DVD
//
