ID A0A1M6APB3_9FLAO Unreviewed; 993 AA.
AC A0A1M6APB3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Predicted Zn-dependent peptidase {ECO:0000313|EMBL:SHI38344.1};
GN ORFNames=SAMN04488508_101403 {ECO:0000313|EMBL:SHI38344.1};
OS Aquimarina spongiae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aquimarina.
OX NCBI_TaxID=570521 {ECO:0000313|EMBL:SHI38344.1, ECO:0000313|Proteomes:UP000184432};
RN [1] {ECO:0000313|Proteomes:UP000184432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22623 {ECO:0000313|Proteomes:UP000184432};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; FQYP01000001; SHI38344.1; -; Genomic_DNA.
DR RefSeq; WP_073313191.1; NZ_FQYP01000001.1.
DR AlphaFoldDB; A0A1M6APB3; -.
DR STRING; 570521.SAMN04488508_101403; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000184432; Unassembled WGS sequence.
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: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:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR PANTHER; PTHR43690; NARDILYSIN; 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};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000184432};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..993
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012206519"
FT DOMAIN 66..116
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 273..441
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 764..890
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 993 AA; 113228 MW; 3708B81EE09DE588 CRC64;
MKIFKSMLLL LFVLLLSNCK DSSTKADTSD VIKTEQHTDS AGFNYETVSN DPTGLRLYTL
DNGMKVYLAK NEEEPKIQTY IAVRAGSNYD PKETTGLAHY LEHMVFKGTD EIGTQDFAKE
KVLLDQISDL YEEHKKESDP EKKKAIYKKI DEVSLEASKI AISNEYDKMI SSLGAQGTNA
HTWFEETVYK NKIPVNELDK WLKVESERFS QLVLRLFHTE LEAVYEEFNR TQDNDFRKSY
YATLEGLFPN HPYGQQRTIG TSDHLKNPSM VSIHNYFNKY YVPNNMAVVL VGDIDFDETI
NKVNDAFGAY EKKEVAHPVL PKEQPITSPV VKEVFGPTSE NVAVAYRSEG IGSEEEKLLT
MADMILTNGK AGLIDLNLNQ KQMVQNAGCS PLFQNDYGFH RFSGTPKNGQ TLDEVKDLIL
GEIEKLKKGE FEDWMMSAVI NDLKLSQTRE YENNTALASA YYNAFIHHQN WEDRVKFLDD
LKKITKQELV DFANKFYQDN YVVTYKRKGE DKNVTKVENP GITPVELNRD KQSKFVSDFY
EIETSPLQPK FIDYKTAIKQ TNTENGLEVS YIKNPNNDLF SLNIIFDMGK DNDRKASLAA
GYLDYLGTDK YSPDELKKEF YKLGINYNVS AGSDITYVGL SGLKENLDAG LALLEHLWGN
AVADQETYNK YVDKIAKARD DNKTQKGNIL WNGLMNYGIY GDNSALRNIY TIAELQEIDP
NELVTKVKEL KGFKHRIFYY GKDVDAAIAS LNKNHVLNGD LADYPEETTY LEKETGGNVY
FVDYDMVQSE MVFLAKGSQF DPSKLAASRL FNSYFGSGLS SIVFQEIRES KSLAYSAFSA
YSNASEKDKS NYIYAYIGTQ ANKMPEAVDA MMDLMTNMPE AEKQFNAAKE ATLKKIAAER
ITKSNIFWSY EGLKKRGIDN DNREEMYNTI KNMTLEDLKK FFNENISGET YNVLVIGNKK
DVDMKALSKL GKVQEMDVDF LFNYEKKKED IKL
//
