ID   A0A1E5AEJ2_9RHOB        Unreviewed;       413 AA.
AC   A0A1E5AEJ2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Type I secretion protein {ECO:0000313|EMBL:OED48534.1};
GN   ORFNames=AB838_11520 {ECO:0000313|EMBL:OED48534.1};
OS   Rhodobacteraceae bacterium (ex Bugula neritina AB1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1868286 {ECO:0000313|EMBL:OED48534.1, ECO:0000313|Proteomes:UP000094333};
RN   [1] {ECO:0000313|EMBL:OED48534.1, ECO:0000313|Proteomes:UP000094333}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB1-7 {ECO:0000313|EMBL:OED48534.1};
RX   PubMed=27681823; DOI=10.1038/srep34362;
RA   Miller I.J., Weyna T.R., Vanee N., Fong S., Lim-Fong G.E.;
RT   "Single sample resolution of rare microbial dark matter in a marine
RT   invertebrate metagenome.";
RL   Sci. Rep. 6:34362-34362(2016).
CC   -!- SIMILARITY: Belongs to the peptidase M10B family.
CC       {ECO:0000256|ARBA:ARBA00009490}.
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:OED48534.1}.
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DR   EMBL; MDLF01000063; OED48534.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E5AEJ2; -.
DR   STRING; 1868286.AB838_11520; -.
DR   Proteomes; UP000094333; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 2.
DR   InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR   InterPro; IPR001343; Hemolysn_Ca-bd.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR   PANTHER; PTHR38340; S-LAYER PROTEIN; 1.
DR   PANTHER; PTHR38340:SF1; S-LAYER PROTEIN; 1.
DR   Pfam; PF00353; HemolysinCabind; 2.
DR   PRINTS; PR00313; CABNDNGRPT.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF51120; beta-Roll; 2.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS00330; HEMOLYSIN_CALCIUM; 3.
PE   3: Inferred from homology;
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          40..195
FT                   /note="Peptidase metallopeptidase"
FT                   /evidence="ECO:0000259|SMART:SM00235"
SQ   SEQUENCE   413 AA;  44370 MW;  FFDE06B07D2E2F55 CRC64;
     MSEVEDYTAL LAYTSNSNYR WNSQVQLGTQ TVVTYSFVGS GELDDVADDP YGATSYWSFN
     NSQRSYFRQA LAEYEEISGL IFVEIDSPAM IDVFGYDGGS AAGWANYAWA SDYYTGNGDL
     AIESSSMAPG TYGYETVLHE IGHAVGLEHP HDGDHTLADH LDDQAHTVMT YTYGGYNVTE
     LGELDAEALQ HLYGDAEGGQ GWNTYVNSSG EVVIKASGRS EIVLATGQDT RVYAFAGNDT
     VKGREADDVL SGGRGEDHVL GGYGEDTLKG GRGADTLIGG VDEGVYSGRN GENDILYGNG
     GRDWLYGGNG DDILRGGLGQ DYLVGGAGSD VLTGGKHADV FVFVSADYWE QNRITDFGTG
     SDRIEISGSI PDSFSDLTIT QQNGNTLINY YGNHDIELTG YTGELTADDF IFS
//