ID A0A0H4WBC2_9BACT Unreviewed; 936 AA.
AC A0A0H4WBC2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:AKQ47811.1};
GN ORFNames=TH63_17860 {ECO:0000313|EMBL:AKQ47811.1};
OS Rufibacter radiotolerans.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Rufibacter.
OX NCBI_TaxID=1379910 {ECO:0000313|EMBL:AKQ47811.1, ECO:0000313|Proteomes:UP000036458};
RN [1] {ECO:0000313|EMBL:AKQ47811.1, ECO:0000313|Proteomes:UP000036458}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG31D {ECO:0000313|EMBL:AKQ47811.1,
RC ECO:0000313|Proteomes:UP000036458};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Rufibacter sp./DG31D/ whole genome sequencing.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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DR EMBL; CP010777; AKQ47811.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H4WBC2; -.
DR STRING; 1379910.TH63_17860; -.
DR KEGG; ruf:TH63_17860; -.
DR PATRIC; fig|1379910.4.peg.3894; -.
DR Proteomes; UP000036458; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000036458};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 43..167
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 200..375
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 527..642
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 672..846
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 936 AA; 102922 MW; 752EF1777B11D649 CRC64;
MQPVNAQATQ KPVAKAAAKP ATNTPGQFNL PFEKYKLANG LEVVLHQDKS DPKVAVAIMY
HVGSNREKPG RTGFAHFFEH MLFQNSENVG KGNFIKNVNQ IGGSFNGGTF TDGTVYYETV
PKDALERILW MESDRMGFFI NTVSEWGLEN EKQVVKNEKR QRVDNQPYGH TNYVILKNLY
PASHPYNWEV IGSLEDLQNA TLADVKEFYN QWYGASNATL VLTGDFETAN AKAMIEKYFG
ELKSKPEVKK LAPMPAKLTA SKSLFHVDNF ANLPELTMVY PTVEQYHKDS YALSMLGSLL
AEGKNSPFER VIVEERKLAP GASAGQSSQE IAGTFRVRVR TFDKKDLDDV QAAIFAAFDR
FEKEGVNEKD LERLKIRQET ALYNGISSLQ NKAFQLAQYN EFAGDPGYAR KDIAMTQAVT
AQDIMNVYLK YIKGKPYVAT SFVPKGQEEL ALKGAVKAEV VEEKVVAGAE GANTGKEPTS
FAKTPSKIDR SKRPALSNNF KFTPPSIWTG QLKNGMKVYG IEQNELPLVN FSVQIKGGMQ
LDDPKKIGTA ALLDAMLLEG TKNKTPQQLE EAIGQLGAYV NVNASTEDIT LTGNTLSRNF
PQVMKLVEEI LLEPRWDEAE FGKAKEAALN RIKQNLANPN AIASLAFNKV LYGQGSRFAY
PTSGTLETVQ GITLQDLKDY YQKNFSPSIA SFQVAGNIKQ ADVTKALVGL EQRWTPKKVT
LPSVVSSPAK PAARLYFIDQ PDAKQSVIYA GYLAVPAGSK DYMALQAINH KLGAGSASTL
FSVLRLQKGY TYGAGSGFSR RPTAPGPFIT SSSVRTNVTK ESLQTIDGIL KDYGTSYSEK
DLATTKGAMF KETALSFETL GSLVNLLETI STYNLPLDYL KQNLTSLQSL SYAQAKSLIS
NYINPNKMVY VVVGDAKTQL SGLKDAGLGK PVVLQP
//
