ID A2TXW3_9FLAO Unreviewed; 437 AA.
AC A2TXW3;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Peptidase family M16 {ECO:0000313|EMBL:EAQ42956.1};
GN ORFNames=MED152_09540 {ECO:0000313|EMBL:EAQ42956.1};
OS Polaribacter sp. MED152.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=313598 {ECO:0000313|EMBL:EAQ42956.1, ECO:0000313|Proteomes:UP000006470};
RN [1] {ECO:0000313|EMBL:EAQ42956.1, ECO:0000313|Proteomes:UP000006470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED152 {ECO:0000313|EMBL:EAQ42956.1};
RX PubMed=17215843; DOI=10.1038/nature05381;
RA Gomez-Consarnau L., Gonzalez J.M., Coll-Llado M., Gourdon P., Pascher T.,
RA Neutze R., Pedros-Alio C., Pinhassi J.;
RT "Light stimulates growth of proteorhodopsin-containing marine
RT Flavobacteria.";
RL Nature 445:210-213(2007).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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DR EMBL; CP004349; EAQ42956.1; -; Genomic_DNA.
DR RefSeq; WP_015481654.1; NC_020830.1.
DR AlphaFoldDB; A2TXW3; -.
DR STRING; 313598.MED152_09540; -.
DR KEGG; pom:MED152_09540; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_1_1_10; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000006470; Chromosome.
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; 2.
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:SF17; PROTEIN YHJJ; 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 Reference proteome {ECO:0000313|Proteomes:UP000006470};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..437
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002646606"
FT DOMAIN 36..181
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 190..367
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 437 AA; 49731 MW; FBD4CE5A87F9D2B2 CRC64;
MKKSILSLAS AVLVAFSMNA QQVEFEEYDL SNGMHVILHQ DSSAPVVVTS VMYHVGAKDE
QPGRTGMAHF FEHLLFEGTE NIKKGEWFKM VSSNGGRNNA NTTDDRTYYY EIFPSNKLEL
GLWMESERLL HPIIGQDGVD TQNEVVKEEK RLRVDNQPYS KFLEYVKENI FKKHPYKGTT
IGKMEDLDAA TLEEFLAFNK KFYVPNNATL VVAGDIDKDA AKKMIEDYFG PIPRGEEITR
NFPKEDPITE QMTAKGYDAN IQIPAIMAAY RTPSMKTRDS RVLDMISSYL STGRSSVLYK
KLVDDKKMAL QAGAINLSQE DYGTYILYGL PQGDTELKDI IAEVDAEIVK MQTELISEKD
FQKLQNQFEN NFVNSNSSVE GIANSLARYN VLYGDTNLIN TEIDIYRSIT REEIRDVAKK
YLNPNQRLLL EYLPEAK
//
