ID A0A163XQP8_9FLAO Unreviewed; 935 AA.
AC A0A163XQP8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Zinc protease {ECO:0008006|Google:ProtNLM};
GN ORFNames=AV926_12585 {ECO:0000313|EMBL:KZE78286.1};
OS Myroides marinus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Myroides.
OX NCBI_TaxID=703342 {ECO:0000313|EMBL:KZE78286.1, ECO:0000313|Proteomes:UP000076630};
RN [1] {ECO:0000313|EMBL:KZE78286.1, ECO:0000313|Proteomes:UP000076630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L41 {ECO:0000313|EMBL:KZE78286.1,
RC ECO:0000313|Proteomes:UP000076630};
RA Hong K.W.;
RT "Whole genome sequencing of Myroides marinus L41.";
RL Submitted (JAN-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:KZE78286.1}.
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DR EMBL; LQNU01000065; KZE78286.1; -; Genomic_DNA.
DR RefSeq; WP_038984473.1; NZ_LQNU01000065.1.
DR AlphaFoldDB; A0A163XQP8; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000076630; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; 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; 3.
DR PROSITE; PS00143; INSULINASE; 1.
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..935
FT /note="Zinc protease"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007847646"
FT DOMAIN 51..174
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 201..371
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 700..864
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 935 AA; 107139 MW; 218A7829168F929E CRC64;
MKRTQILYFF ASVLCPLLAV GQSTFSDLPK ADKAIYGTLD NGLNYIIHPI PQQKTEYRLV
LNVGSLQERD DEKGFAHFLE HMIFNGSDDF PGRQAIDTLQ RLGYQFGRDI NAYTTYERTV
YDLSLLDIRQ QDLAINILGN FLGKSHLNKE GIEKERRIVI QEIKDFGTEP LFNRKKLENT
PHANRLPIAT ESDILNLDPI KLKAFYQRWY NPTLATIIIV GNVNTTEAVE QIKKHFGAFK
GQSNLTRTQS ENTFSPTYTD RLEVQKDSNA TANKLEIIRF SDAPFLANKA DYKQQVIEQV
YKLWLNHKLS QAKSQTTAHS LWYLPNKNEN ALELKAKTKE ELYSGINLTA SVLNTMTVKG
IHNEELTRFK QHLLNHSTPT TDEDITYVTN AYVDQVVVNS HYISSVDRHR LLEEVLPEIT
REDINQKHTA IWDTSKENLY LLTANDRLFS IESAEELDQQ WSEGATKTLV FKKAKKKKSH
HRPKGAFHWK VMPPIHSENT GTITAEKYYD NLDITELTLS NGLRIGIKPT KATDDNYILT
MFTRNGLSQI PTDERKYYQD ASYFIDSSWI HGLTHDGYMS VGADREISTL VSINNDASII
NTSSRKGNTR DLFEWTYRKL YDYIKPKQDF KEYVEESIAA IDTTTAPSSL LSNPSIQIEH
QIEAYKKGTL LSSEELTTAE DWQKVNLDNF FSLYNQSFAN LNEVYVLIAG NFNAEEIKTK
ALRYFGSLED HTNKVSQENR NSLKSPLKEV KRVTLSSSDV ERTDVTIVFN GTIQPVLKES
MMAHIVREMF NNQFLTLSRE KEGLVYSPSS VLEVEIYPNP RTSVSLFFSA TLSDVEKLEQ
LAMEVINSIQ TQRISESELG QMKRTILNNK KLHLTETSTF QWVDKLRETQ LNFSSLKDFN
DYETILNSIT PDDLIKVAKS MFTTSSYGVF LVTPK
//