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Database: UniProt
Entry: A0A2M9AQF0_9BACT
LinkDB: A0A2M9AQF0_9BACT
Original site: A0A2M9AQF0_9BACT 
ID   A0A2M9AQF0_9BACT        Unreviewed;       441 AA.
AC   A0A2M9AQF0;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN   ORFNames=CLV45_4602 {ECO:0000313|EMBL:PJJ47912.1};
OS   Hymenobacter chitinivorans DSM 11115.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1121954 {ECO:0000313|EMBL:PJJ47912.1, ECO:0000313|Proteomes:UP000228535};
RN   [1] {ECO:0000313|EMBL:PJJ47912.1, ECO:0000313|Proteomes:UP000228535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11115 {ECO:0000313|EMBL:PJJ47912.1,
RC   ECO:0000313|Proteomes:UP000228535};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): From Individual Species to Whole Genera.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU362031};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the peptidase M50B family.
CC       {ECO:0000256|ARBA:ARBA00007931, ECO:0000256|RuleBase:RU362031}.
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:PJJ47912.1}.
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DR   EMBL; PGFA01000005; PJJ47912.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M9AQF0; -.
DR   Proteomes; UP000228535; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00989; PDZ_metalloprotease; 1.
DR   CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR   Gene3D; 2.30.42.10; -; 2.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004387; Pept_M50_Zn.
DR   InterPro; IPR008915; Peptidase_M50.
DR   NCBIfam; TIGR00054; RIP metalloprotease RseP; 1.
DR   PANTHER; PTHR42837:SF2; MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR42837; REGULATOR OF SIGMA-E PROTEASE RSEP; 1.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362031};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362031};
KW   Metal-binding {ECO:0000256|RuleBase:RU362031};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU362031};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:PJJ47912.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362031};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362031};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU362031}.
FT   TRANSMEM        34..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        106..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        374..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        419..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   DOMAIN          216..281
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
SQ   SEQUENCE   441 AA;  48492 MW;  F2C8EE82866F43DD CRC64;
     MAGQMLLGLS ILVGLHEFGH FAAAKYFKIR VDKFYIFFDF LFPMPGVMNF ALFKKKIGET
     EYGLGWFPLG GYVAIHGMID ETQDAESLSA EPQPNEFRAK PAWQRLIVML GGIIMNVITG
     ILIFTALTAN YGESYLPASE VRYGVVPNKL GEEMGFRTGD KIVKINGRPF TEFDQVYSPD
     VMLGNNSYYT VDRNGQLLDI AIPKNFMDRL SDKDQTPFVL PLNPFVVGQV VSGSGAAKGG
     LLPNDRILTV AGKTTQFFPE LQEALKANAG KTVPVQVTRA GQPVTLQIAV DEEGHIGFMP
     KSLLKEATRT YGLAASLPVG TKKAFGVITT QMKAFGKIFS GNASFSKSIG GPVEIAQQYG
     GQWEWERFWT LTGMLSMVLA FMNLLPIPAL DGGHVVFLLY EMIAGRKPSD TFMENAQKVG
     MVMILGLMAY VLIIKQVLKL F
//
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