ID A0A0N1L7W7_9SPHN Unreviewed; 948 AA.
AC A0A0N1L7W7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:KPF62090.1};
GN ORFNames=IP79_14025 {ECO:0000313|EMBL:KPF62090.1};
OS Porphyrobacter sp. AAP60.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Porphyrobacter.
OX NCBI_TaxID=1523423 {ECO:0000313|EMBL:KPF62090.1, ECO:0000313|Proteomes:UP000037996};
RN [1] {ECO:0000313|EMBL:KPF62090.1, ECO:0000313|Proteomes:UP000037996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP60 {ECO:0000313|EMBL:KPF62090.1,
RC ECO:0000313|Proteomes:UP000037996};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:KPF62090.1}.
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DR EMBL; LJHV01000023; KPF62090.1; -; Genomic_DNA.
DR RefSeq; WP_054120017.1; NZ_LJHV01000023.1.
DR AlphaFoldDB; A0A0N1L7W7; -.
DR STRING; 1523423.IP79_14025; -.
DR PATRIC; fig|1523423.3.peg.1701; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000037996; 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}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..948
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005876587"
FT DOMAIN 63..201
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 220..393
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 527..654
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 677..857
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 469..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 948 AA; 101062 MW; 62507202FEE83E08 CRC64;
MTSRFAAASL SALAFALAVP FAPALADNHA ATAAPQATAD LPALVAQVQI PYEEFQLDNG
LTVIVHEDRK APVVGVAVWY NVGSKDEPKG QTGFAHLFEH LMFNGSENAP DDYFQYLAEM
GATDYNGTTN FDRTNYFQTV PRPALERALW LESDRMGYLL GAVTQEKLDN QRGVVQNEKR
QGDNQPGGLV FYELLATMFP EGHPYHHSVI GSMADLDAAS MDDVRKWFTD KYGPNNATLV
MAGDISAAEA RVLAEKYFGP IARGPVNTPA AADVPMLAQD VRKVMKDQVA ATNVTRYWPG
PGITDADLTA LNVGAAILGG LASSRLDEVL VRDEQLAVGV SASSSNFQRV GLLSVSATAK
PGVDLAVLEA RLDELVAKFI AEGPTEDEVR RAATSSLART VRGLEQVGGF GGKAVTLANG
EVLAGDASFY ATQLERLAKV TPADVKDAMA RWMTRPAFTL VLEPGERDGS YEEAASVGGD
ANASERDREA ETLTVTLERP KPAIDTTAEL DFPDVERATL KNGMKVTYAR RTAVPATYVT
MSFNAGGAAD PAGKAGLQDM TMNLFTEGTA SLTGQQIAEA SERLGVSINS GGSDDRSSFT
MSALTANLAP SLDLMRQIMR EPAFNPADLE RVRTQTVTGI RQSMKSPQGI AQRTLAPELF
GAQSAYGGVN TVESVSSITR EDLVAFKDSW IRPDNGEVFV ISDRPLTEIV TALNASFGDW
KAPAAAKGTK QVTATQAGAG NRIILVNRPN SPQSFIIGAQ VTPLDAGDPG FIAFNSANNS
LGGNFLARLN MNLRETKGWS YGVRGGTQAR ENAVVYAISG GVQADRTGDS LAEMLRETKE
FLTEKGVTAA ELDRSIASSV GALPGQFETS PAVLGAMQGN ALFGRPDNYQ ETLASIYRAQ
TTESLDAAAR AAIDADKFVW VVVGDASKVR AQLEPLGLPI EQREMEGE
//