ID A0A1N7LWL4_9FLAO Unreviewed; 953 AA.
AC A0A1N7LWL4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Zinc protease {ECO:0000313|EMBL:SIS78091.1};
GN ORFNames=SAMN05421785_102541 {ECO:0000313|EMBL:SIS78091.1};
OS Chryseobacterium gambrini.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=373672 {ECO:0000313|EMBL:SIS78091.1, ECO:0000313|Proteomes:UP000185781};
RN [1] {ECO:0000313|EMBL:SIS78091.1, ECO:0000313|Proteomes:UP000185781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18014 {ECO:0000313|EMBL:SIS78091.1,
RC ECO:0000313|Proteomes:UP000185781};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FTOV01000002; SIS78091.1; -; Genomic_DNA.
DR RefSeq; WP_076390979.1; NZ_FTOV01000002.1.
DR AlphaFoldDB; A0A1N7LWL4; -.
DR STRING; 373672.SAMN05421785_102541; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000185781; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF34; ZINC PROTEASE PQQL-LIKE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SIS78091.1};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..953
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012388001"
FT DOMAIN 45..163
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 201..384
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 691..861
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 953 AA; 107545 MW; E7214CE678A68D3B CRC64;
MKKMFSSLAV VVLMSANAFA QNIPMDPSVK TGTLPNGMKY YIRKNTLPEK KVDFRLAINA
GSILEDENQR GLAHFMEHMN FNGTKNFPDN KLVDFLQSIG VKFGQHLNAY TSFDETVYML
PVPLDKPGNL DAGLKVMEDW AFNATLSDEQ INKERGVVLE ELRLGLGADK RMSDKYLPKL
LYNSQYANRL PIGKKDVLEN FKPDVIRQFH KDWYRPDLMA IVVVGDINVD EVEKKIKDNF
SKYKNPSKPR ERKSFDLPNH KETLVAIETD PDATRSMVQF IMKDSESYQP DVTVEQYNQS
LVEQIASTML NNRLGELVNS NNPPFTYGYV YHGGTYARSK EAFQGMAMVK DGNQLNALKV
LLEETERAKR FGFTQTELDR AKAQVMSNIE RTYNNRDKTE SDVLVDEYVR NFLEQEPMPG
IAWEYEDTKK FLPSVTLAQT NEVFKKLVKD DSRVVVITGP KKDNIQMPTE AMVLNTFEGV
KMADLKPYQE KATIKNLVKP FKSEGAIAKT ENDAKLGTTT WTLSNGAKVT FKKTDFKDDE
IVFAARSLGG SSVINDADFI KTQFAFPALS EAGVNGFSKA DLTNYLAGKQ VNVNPSIGNV
TEGLSGRTTR KDLGTAMELM YAYFTGLNYN PDAFNAYKTK QSAMMDNLLS NPQFYFSSEH
AKFMNQKNPR FVGIIPVEKD WANTDYKKAY DIYKEKFSNA GNFQFYFVGN IDEATFKNEV
LQYIASLPSS GKTSTFKDTG YRQITGDYSK VYKKGKDPKS MVTIAYSGEA PYNEKEALAL
EALGEVATIK VIEKLREDES GIYGGGARGG MYKVPFSNYS FSINFPCGPE NAEKLTKSAI
TELQKLIDKG PEQKDLDKYK EGEYNDDKTN MKDNMYWMNA LTKNQLDGSD KYEILNYQEK
VKALTVKDLQ DVAKKYLTKG RIVATLMPED GWEKAKKEEA KAETAVIKAG AAK
//
