ID A0A117SDA4_9FLAO Unreviewed; 950 AA.
AC A0A117SDA4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:KUO65031.1};
GN ORFNames=APF83_10860 {ECO:0000313|EMBL:KUO65031.1};
OS Lutibacter sp. BRH_c52.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lutibacter.
OX NCBI_TaxID=1734397 {ECO:0000313|EMBL:KUO65031.1, ECO:0000313|Proteomes:UP000054346};
RN [1] {ECO:0000313|EMBL:KUO65031.1, ECO:0000313|Proteomes:UP000054346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c52 {ECO:0000313|EMBL:KUO65031.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-2015) 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:KUO65031.1}.
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DR EMBL; LOEY01000067; KUO65031.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117SDA4; -.
DR Proteomes; UP000054346; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF21; PROCESSING PROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 2.
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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 51..175
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 208..386
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 530..656
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 679..855
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 950 AA; 107284 MW; 10D452EBE579B4DC CRC64;
MIKINLKTSI LALLTLSFMV ISFKGISQNS SKDVKFSIAF EKYELSNGLD VVLHQDKSDP
IVSLAIQYGV GSNREITGRT GFAHLFEHML FQESENVPQD QFFKKIQDVG GTLNGGTWKD
GTVYYEVVPN NALETVLWLE SDRMGFLINT VTESAFNNQQ EVVQNEKRQR VDNNPYGHTN
WVLDKNIYPA GHPYSWQVIG ELEDLQNATV DDVKEFYNRF YGPNNATLVL AGDFEIKDAK
ALIEKYFGEI KRREEVKRLE PQPVTIAETK RFYHEDNFAT APQLNMVWPT LQQYTADAYA
LDFLAEILSS GKKAPLYKIL VKENNLTSRT SAYNNSQELA GEFHINITAN AGNNLKDVEK
GIFEAFDLFE KEGITDKDVE RIKAGLETSF YNGISSVLGK SFQLARYNVF AGTPGFIEQD
IENIKKVTKE DVIRVYEKYI KGKPYIMTSF VPKGKLDLIT ENSKKAEVVE EEIKENVVKT
IVDVKEEIVK TPSAIDRSKE PNQGISPKLS IPKSWTSTLS NKMKVYGIEQ NEIPTVNFSL
VIAGGHLLDN KNKNGVANLM TDIMMEGTAN KTPEQLEEEI EMLGASINMY TTNESIVLRG
NTLVRNFDKT IKLIEEILLE PRWDEEEFLR IKTKTINQIK RSDANPNVVA DNVFNKILYG
ENHIFSYPTS GTETSVEAIT MEDLKAFYKA NFSPSVSVFN IVGNITKEQI LKNLSGLENR
WKAKNVQIPE FPITNTRDKA SLYFVDIPNA KQSVINIGYI GLARTDKDFY PAEVMNYKLG
GSFSGNVNLI LREEKGYTYG ARTGFSGSKT PGTFLASSSV RTNTTGESVQ IFKDEIAKYK
NGISKEDLEF TKNALIKSNA RRFETQTSLL GMLQEISNYN LPSNYIEKEE ATINNMTLEQ
HKQLANKYLD ESKMVYVVVG DAATQFAQFK TMGFDEVKLK TKDAKEVIIE
//
