ID A0A199XNS0_9FLAO Unreviewed; 945 AA.
AC A0A199XNS0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Protease 3 {ECO:0000313|EMBL:OAZ02994.1};
DE EC=3.4.24.55 {ECO:0000313|EMBL:OAZ02994.1};
GN Name=ptrA_2 {ECO:0000313|EMBL:OAZ02994.1};
GN ORFNames=FLB_26680 {ECO:0000313|EMBL:OAZ02994.1};
OS Flavobacterium succinicans.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=29536 {ECO:0000313|EMBL:OAZ02994.1, ECO:0000313|Proteomes:UP000093807};
RN [1] {ECO:0000313|EMBL:OAZ02994.1, ECO:0000313|Proteomes:UP000093807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD5b {ECO:0000313|EMBL:OAZ02994.1,
RC ECO:0000313|Proteomes:UP000093807};
RA Poehlein A., Daniel R., Simeonova D.D.;
RT "Draft genome sequence of Flavobacterium succinicans strain DD5b.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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:OAZ02994.1}.
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DR EMBL; JMTM01000070; OAZ02994.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A199XNS0; -.
DR PATRIC; fig|29536.5.peg.2764; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000093807; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
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; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF34; ZINC PROTEASE PQQL-LIKE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OAZ02994.1};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:OAZ02994.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000093807};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..945
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008286724"
FT DOMAIN 58..177
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 215..397
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 705..874
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 945 AA; 107714 MW; 7FF895FA6A481C24 CRC64;
MLSTKHIFMK KFNQFALGIM LFPVAILAQT MDYGQAIPFD PNVKTGKLDN GLTYYIKKNA
KPEKKVDLRL VVNAGSILED DDQQGLAHFM EHMCFNGTKR FPKNQLVDYL QSIGVKFGQH
LNAYTSFDET VYFLPIPSDN PEKLEKGFQI LEDWAFNTVL TPEEIDKERG VVLEEYRLGL
GAQKRMMGRY LPKMMYNSKY ANRLPIGQKE ILEKFKYETL TRFYKDWYRP NLMSVIVVGD
IDVAEMEKKI KEHFSAYKNP ANEKVRNVFE VPNHKETFVA VESDKEASNT QVQLVYKDYD
APKKITTIGD FRSYLVEGLF TTLLNNRLEE LTNSATPPFT FGYSYYGGTY ARTKKAYQSV
AMMAEDKQLS ALKVLVTENE RARKFGFTSG ELDRAKADFL AQIEKNYNDR TKTDSENFVE
EMQLNFLEQE PLPGIEWTFE TMKKILPTIA LADVNGFIKN YIKEDNRVVV FTGPQKDNLK
KVTEQEVLET LKVNEADLKP YEDKAVATSL LRKEAKAGTI VKREANATLG TKTLVLSNGV
KVVYKTTDFK NDEVLFEAVS LGGSNLYSNE VMKKVQFANG ALAEAGFSGL KLNDINKFMT
GKIARVNPYI GQTTEGLRGN TTPKDLEYLF QMVHAYFTDL NFDPEAFEGF KQKQASFFKN
MASQPQYYFQ QEFYTYLNKE NPRFNGIMPT DKSWAETDYK LAYDKYKERF ANAADFEFFF
VGNVDDKTIE AFATKYLASL PTTAAKEKTV DLGYRMLKGD LKKVVNKGTD PKSNVNIMFY
GEAKYSPKEA LAIEALGEVL TIKLIEQLRE SESGVYGVSA RGSMNKVPYG SYNFTINFPC
GPDNAEKLTA SALNELQKII TNGPEEKDVA KYKEGELADY RKDSKENRFW LTNFTRSFLY
GSNPENALKY EAEVNAITAK DIQEVAKKYL TKDKVIGMLM PESKS
//