ID   A0A254R0V1_9RHOB        Unreviewed;       438 AA.
AC   A0A254R0V1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Zinc protease {ECO:0000313|EMBL:OWU80837.1};
GN   ORFNames=ATO1_06790 {ECO:0000313|EMBL:OWU80837.1};
OS   Phaeobacter sp. 22II1-1F12B.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Phaeobacter.
OX   NCBI_TaxID=1317111 {ECO:0000313|EMBL:OWU80837.1, ECO:0000313|Proteomes:UP000197279};
RN   [1] {ECO:0000313|EMBL:OWU80837.1, ECO:0000313|Proteomes:UP000197279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22II1-1F12B {ECO:0000313|EMBL:OWU80837.1,
RC   ECO:0000313|Proteomes:UP000197279};
RA   Lai Q., Li G., Shao Z.;
RT   "Phaeobacter sp. 22II1-1F12B Genome Sequencing.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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:OWU80837.1}.
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DR   EMBL; AQQP01000004; OWU80837.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A254R0V1; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000197279; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851:SF149; GH01077P; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:OWU80837.1};
KW   Protease {ECO:0000313|EMBL:OWU80837.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000197279};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..438
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013191326"
FT   DOMAIN          38..174
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          186..361
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   438 AA;  47472 MW;  456EA81A860BD55B CRC64;
     MKRLFVSLIL LIVAVPAWAE IDIQKVTSEK GITAWLVEEH SIPFTALELR FRGGTSLDEP
     GKRGATNLMA ALLEEGAGDL DAREFARRKE ELAASFGYGA SDDSVSVSAK FLSENRDEAL
     ALLRTTLMEP RFDEDALERV RAQVISGLMS DAKDPNTIAG NAFSEMAFGD HPYGSSGDGT
     IETVTSLTRE DIQTAFDNVF ALDRIYVSAV GDITPEELSA LLDELVGDLP ETGAPMPGPA
     NVAITGGNTI VDFDTPQSVA VFGQTGMARE NDDFFAAYVM NQILGAGGFE SRLMTEVREK
     RGLTYGVYSY LAPKTWGPIY VGRVSSSNDR IAEAVQVIRD EWSKLSEEGV TQKELDDAKT
     YLTGAYPLQF DGNGQIASIL VSMQVNGLPI DYVTTRNAKM EAVTLEDVNR VAREFLDPEN
     LHVVVVGKPE GMEATAGN
//