ID A0A2W7K5J1_9FLAO Unreviewed; 951 AA.
AC A0A2W7K5J1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=Putative Zn-dependent peptidase {ECO:0000313|EMBL:PZW42730.1};
GN ORFNames=LX95_01047 {ECO:0000313|EMBL:PZW42730.1};
OS Mesonia algae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Mesonia.
OX NCBI_TaxID=213248 {ECO:0000313|EMBL:PZW42730.1, ECO:0000313|Proteomes:UP000249542};
RN [1] {ECO:0000313|EMBL:PZW42730.1, ECO:0000313|Proteomes:UP000249542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15361 {ECO:0000313|EMBL:PZW42730.1,
RC ECO:0000313|Proteomes:UP000249542};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:PZW42730.1}.
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; QKYV01000002; PZW42730.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W7K5J1; -.
DR Proteomes; UP000249542; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
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; 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; 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:UP000249542};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..951
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016141624"
FT DOMAIN 53..176
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 204..393
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 713..881
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 951 AA; 111389 MW; CE9BD6672A8CF285 CRC64;
MIQLKKRLPS LIWVLLFISS IVQAQEGIKE IESLRSGTLP NGFQYFIKDV ENPVAKTTMR
LYIKAGFDHE DSLQQQMSHL IEHLAFKPTL HTPTSIKDEA FLDRLGMNFR DIGGTTSNLH
TRYLFDAPPN HPKAFQTGLA WFKDIAMRLP LTSEHINQEK GSVWQELISG NQDYQDYYKA
ERNLEAQLFP FRQSYDQLSQ HIQNFSHKEL RRFYKDWYRP DLMAIVVVGN LNDMQETEKL
IQDTFSDIPT PQASYPHIDI HSAQQKRSPQ FKTQVWEKGF DPEKKEEVEY HWYIRQPELV
NSLHTREGYK RYIAFQLLSR VLHQRLKEAN APALIGSAKN KDTYSYGGNP FSLALYFTTF
PSKSKEAFQQ IAMPLLQLKE QGVKEQEWKK IKEDYLKESL QSEVFYWNEE LRDYWLKNEV
LFPNKQKVFH QWVQELSIEK MNAYLPQFLS SPPKDIGIIA PQGNKALNFT EEEIRAWVEE
AYRGPVPMYQ PPKVVKSLYN EIQKEELPLV AYTTKAPAIP ETQEIVLSNG VRVVLKPYQP
TPGVGEQSIK ISGFSLRGAA CYSSSDYYSA LNATDLVTHQ GVGGINAKEI QSLMDYAEIM
NCRSYIDYKE SSLQAEGNLK HTEEILQLLS LYFQPVNPQD IDFDAWQKEA LETRKSQKNI
QEDFRNVIRK VVQDSAIPPS FNFRYLKGEQ AILSIGKTEE KRSLEIYQHV FGKPEQWTFL
ITGNFKTEDV IPLLQRYLGN IKPTVQKLRC TPTRQKTFKA SGPVKKEILS NIPMENGMYD
ASYYQEQKGK NSWKETLELR VLGQVIQRKL NRLRYEKGFS VYNFGGYGRY DPEVKRYRLY
FQVACHPKEL YPIQKEIQFI VKELRAGEIP KEYLKQAKQN MKRRYNVSYL KQHRQLHELL
FQHLRYEEAW VPLEKYETFI DNIEMEDMVR LSKKYLKEKN KIEVIMSDEA L
//
