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Database: UniProt
Entry: A0A1Y2JZY6_9PROT
LinkDB: A0A1Y2JZY6_9PROT
Original site: A0A1Y2JZY6_9PROT 
ID   A0A1Y2JZY6_9PROT        Unreviewed;       647 AA.
AC   A0A1Y2JZY6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Putative M23 peptidase domain-containing protein {ECO:0000313|EMBL:OSM00104.1};
GN   ORFNames=MAIT1_00529 {ECO:0000313|EMBL:OSM00104.1};
OS   Magnetofaba australis IT-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales;
OC   Magnetococcaceae; Magnetofaba.
OX   NCBI_TaxID=1434232 {ECO:0000313|EMBL:OSM00104.1, ECO:0000313|Proteomes:UP000194003};
RN   [1] {ECO:0000313|EMBL:OSM00104.1, ECO:0000313|Proteomes:UP000194003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IT-1 {ECO:0000313|EMBL:OSM00104.1,
RC   ECO:0000313|Proteomes:UP000194003};
RX   PubMed=27801294; DOI=10.1186/s12864-016-3064-9;
RA   Araujo A.C., Morillo V., Cypriano J., Teixeira L.C., Leao P., Lyra S.,
RA   Almeida L.G., Bazylinski D.A., Vasconcellos A.T., Abreu F., Lins U.;
RT   "Combined genomic and structural analyses of a cultured magnetotactic
RT   bacterium reveals its niche adaptation to a dynamic environment.";
RL   BMC Genomics 17:726-726(2016).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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:OSM00104.1}.
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DR   EMBL; LVJN01000021; OSM00104.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2JZY6; -.
DR   STRING; 1434232.MAIT1_00529; -.
DR   Proteomes; UP000194003; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd12797; M23_peptidase; 1.
DR   Gene3D; 3.10.450.350; -; 3.
DR   Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR   InterPro; IPR045834; Csd3_N2.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR016047; Peptidase_M23.
DR   PANTHER; PTHR21666:SF272; BLL1407 PROTEIN; 1.
DR   PANTHER; PTHR21666; PEPTIDASE-RELATED; 1.
DR   Pfam; PF19425; Csd3_N2; 1.
DR   Pfam; PF01551; Peptidase_M23; 1.
DR   SUPFAM; SSF51261; Duplicated hybrid motif; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194003};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..647
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012711496"
FT   DOMAIN          372..493
FT                   /note="Csd3-like second N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19425"
FT   DOMAIN          506..602
FT                   /note="Peptidase M23"
FT                   /evidence="ECO:0000259|Pfam:PF01551"
SQ   SEQUENCE   647 AA;  70088 MW;  775D8D83F2791EF7 CRC64;
     MVAVSSVRRR RLIVRSVAAA ALFLSALAIN SALDANTGGE TGNAPPRITT SAQMTQLAQQ
     TAGQIVAEEA NGVSLLSGQP LETLLDSEAD YAQGAEPQLE FSQSPDEAPV GHPLQTALKR
     ERGEVRPGDS FSGLMERLNA PYLTAIEISR ASKPVYDIAT RLRPGKPLEA HYSADGQLQA
     FFYAVTDDKT LAVRRNDDGR FTARMMRLTL EAAANGPAQT VTADAGTARS APDPLIRPIP
     AATPSPRKAR MLAARMNDPK RRAASALTPP PADHAVARLV EETVRNGDHL AAVLARADVT
     APTALSVAES ARSVYDLARK LKPGKTLQLA FDKQGQLVEL SYPVSKISSL VLSRVDGDGF
     RAVLDKPELD MRMRSVSGTV NGSLFIAARR AGLSQPLAVK LAGLFEWDVD FARDIRAGDR
     FTVIYEEYRH DGKKVRDGDI VAARFVNQGN VFEAFRFTDG NGDTGYYDSK GNNVQKMFIR
     APVDYTRISS RFSKARKHPI LGFTRAHKGV DYAAPTGTPI RAAGNGRVIY RAYKGGFGNL
     VLIRHNSTYT TAYAHMSRYA RNLKPGSRVR QGQVIGYVGA TGKATGPHLH YEVRVRGVQV
     NPLSVKLPSA RSLPRSLMPK FRQQRLALVA RLNNASPTVL AALKKEG
//
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