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Database: UniProt
Entry: U4V510_9RHOB
LinkDB: U4V510_9RHOB
Original site: U4V510_9RHOB 
ID   U4V510_9RHOB            Unreviewed;       441 AA.
AC   U4V510;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Putative Zn-dependent peptidase {ECO:0000313|EMBL:ERL97776.1};
GN   ORFNames=HIMB11_01727 {ECO:0000313|EMBL:ERL97776.1};
OS   Rhodobacteraceae bacterium HIMB11.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1366046 {ECO:0000313|EMBL:ERL97776.1, ECO:0000313|Proteomes:UP000016848};
RN   [1] {ECO:0000313|EMBL:ERL97776.1, ECO:0000313|Proteomes:UP000016848}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HIMB11 {ECO:0000313|EMBL:ERL97776.1,
RC   ECO:0000313|Proteomes:UP000016848};
RA   Durham B.P., DeLong E.F., Rappe M.S.;
RT   "Draft genome sequence of marine alphaproteobacterial strain HIMB11, the
RT   first cultivated representative of a unique lineage within the Roseobacter
RT   clade possessing a remarkably small genome.";
RL   Submitted (AUG-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:ERL97776.1}.
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DR   EMBL; AVDB01000005; ERL97776.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4V510; -.
DR   STRING; 1366046.HIMB11_01727; -.
DR   PATRIC; fig|1366046.3.peg.1752; -.
DR   eggNOG; COG0612; Bacteria.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000016848; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; 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; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   PANTHER; PTHR11851:SF229; PEPTIDASE M16 DOMAIN PROTEIN; 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   Reference proteome {ECO:0000313|Proteomes:UP000016848};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..441
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004657026"
FT   DOMAIN          38..183
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          191..375
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   441 AA;  48978 MW;  6EFEDF7339570B57 CRC64;
     MILRLFLSFC VGLTFVTASH AAIEDQVSEF MLDNGMQVVV IEDHRAPVVV HMVWYRAGAA
     DETPGVSGVA HFLEHLLFKK TKILAAGELS RTVAENGGTD NAFTSYDYTA YYQRVAADRL
     PIMMQMEADR MVNLDLTEDD ILVERDVIIE ERNQRTETNP SALYREQANA ALFQNHRYGV
     PVIGWRHEMS NLTLSDALAY YKQFYAPNNA VLIVAGDVVP DEVLSLAKST YGKIPANPNL
     SDRKRPIEPP HFAPRRIEYV DERVSQPYVV RSYLAPERNS GDQRPAAALA LLADILGDGQ
     ASVLQRKLQF ETQEALYASA SYLGVSLDTT SFAVYIVPSA DVSLEDAEAA LDRAIAEFME
     EGVDDAQLDR LKTQYRAAGI YAQDSVNGLA NAYGRALTSG LTLQDIHEWP DIIQSVTVEE
     IMTAARDVFD LNSSVTGWIR K
//
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