ID K1LX78_9LACT Unreviewed; 568 AA.
AC K1LX78;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=M3 family oligoendopeptidase {ECO:0000313|EMBL:EKB54653.1};
GN ORFNames=HMPREF9706_00843 {ECO:0000313|EMBL:EKB54653.1};
OS Facklamia hominis CCUG 36813.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Facklamia.
OX NCBI_TaxID=883111 {ECO:0000313|EMBL:EKB54653.1, ECO:0000313|Proteomes:UP000004465};
RN [1] {ECO:0000313|EMBL:EKB54653.1, ECO:0000313|Proteomes:UP000004465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 36813 {ECO:0000313|EMBL:EKB54653.1,
RC ECO:0000313|Proteomes:UP000004465};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Facklamia hominis CCUG 36813.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|RuleBase:RU003435}.
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:EKB54653.1}.
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DR EMBL; AGZD01000007; EKB54653.1; -; Genomic_DNA.
DR RefSeq; WP_006908164.1; NZ_JH932292.1.
DR AlphaFoldDB; K1LX78; -.
DR STRING; 883111.HMPREF9706_00843; -.
DR MEROPS; M03.010; -.
DR PATRIC; fig|883111.3.peg.841; -.
DR HOGENOM; CLU_030403_1_0_9; -.
DR OrthoDB; 9769691at2; -.
DR Proteomes; UP000004465; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09606; M3B_PepF; 1.
DR Gene3D; 1.10.1370.30; -; 1.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR InterPro; IPR011976; Pept_M3B_oligopep-rel.
DR NCBIfam; TIGR02289; M3_not_pepF; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000004465};
KW Zinc {ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 166..543
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 568 AA; 66687 MW; DF3CC8271E566B97 CRC64;
MKFASFKYER PQLDQVKEQF YQAIHQIKEA TSLEALKEAI QAVRQIQNNL ATQGTLCSIR
HSIDTKDDFY SQETDFWDEH YPLIANWEKD YYQAVLENEL SQSLKGDFLP EPFFAIAENQ
LRTNSEAVIP LLQEENRLVS EYGKLKASAE IEFKGQVYNL SSIGAFTQSA DRLERKEAFE
KISAWYQKHQ DDFDRIYDQM VKVRHEIAKK LGFKDFVELG YARMLRLDYD RQDVERYRQE
VIKYVVPLAE KLVQAQKERL NLDHLAYYDL GLMFPKGNAN PSGTSQEIVD KAQTMYHELS
KETGEYFDFM RSGDLLDLES KPGKDTGGYC THLPNYKAPF IFANFNGTSH DVEVLTHEAG
HGFQVYSSMW IETPEVVWPT YETCEIHSMS MEFLTWPWME NFFQESTAKF KYQHLAGALM
FIPYGCLVDH FQHEVYEHPE WTPQERRQAF RRLEKIYNPW IDYEGNDFYE QGGLWFKQLH
IFTMPFYYID YTLAQVCAFQ FWKRDHVDHD SKTWEDYVRI CRLGGTKTFT QVVAAANLKS
PFEPGNLEET VASIDQYLSA VDPQALLK
//
