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Database: UniProt
Entry: A0A0P7Y9R3_9RHOB
LinkDB: A0A0P7Y9R3_9RHOB
Original site: A0A0P7Y9R3_9RHOB 
ID   A0A0P7Y9R3_9RHOB        Unreviewed;      1124 AA.
AC   A0A0P7Y9R3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Integrin, beta chain {ECO:0000313|EMBL:KPP84658.1};
GN   ORFNames=HLUCCO07_06030 {ECO:0000313|EMBL:KPP84658.1};
OS   Rhodobacteraceae bacterium HLUCCO07.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1666914 {ECO:0000313|EMBL:KPP84658.1, ECO:0000313|Proteomes:UP000050369};
RN   [1] {ECO:0000313|EMBL:KPP84658.1, ECO:0000313|Proteomes:UP000050369}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLUCCO07 {ECO:0000313|EMBL:KPP84658.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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:KPP84658.1}.
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DR   EMBL; LJSU01000024; KPP84658.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7Y9R3; -.
DR   STRING; 1666914.HLUCCO07_06030; -.
DR   PATRIC; fig|1666914.4.peg.1427; -.
DR   Proteomes; UP000050369; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
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:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
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; 3.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR   InterPro; IPR001343; Hemolysn_Ca-bd.
DR   InterPro; IPR002369; Integrin_bsu_VWA.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR013858; Peptidase_M10B_C.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR38340; S-LAYER PROTEIN; 1.
DR   PANTHER; PTHR38340:SF1; S-LAYER PROTEIN; 1.
DR   Pfam; PF00353; HemolysinCabind; 3.
DR   Pfam; PF00362; Integrin_beta; 1.
DR   Pfam; PF08548; Peptidase_M10_C; 1.
DR   PRINTS; PR00313; CABNDNGRPT.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF51120; beta-Roll; 2.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS00330; HEMOLYSIN_CALCIUM; 4.
PE   3: Inferred from homology;
KW   Integrin {ECO:0000313|EMBL:KPP84658.1};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          20..205
FT                   /note="Peptidase metallopeptidase"
FT                   /evidence="ECO:0000259|SMART:SM00235"
FT   REGION          648..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        678..692
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1124 AA;  117039 MW;  06A29632570C16C4 CRC64;
     MAGSRTVDAN TNTLLAGLQR TNQWDTGNLT YWIAEAGDSD RIDEIYEEKY EEEPGAGNAH
     EPINDTTAPA WNDAIDNALY HISLATGLDF SEDSGIDTAD IVFSGGYPDT DGVVAWMNGP
     GSILKPGETD DYQSFLTNRM GNAGWDEEAE TGGGSFADFV ILHELGHGLG LSHPHNDDSG
     TTAWTNGDAV STDNKADNAR YTVMSYEIGG IDTQVFDNFG NNVTLGALDI AALQDVYGAP
     DAHTGDTTYT LTDERSTARD LDGTDGSVSI GRAFYSIWDT GGTDEIDYSG SNNAYINLQD
     ASLVQEARSA DADILKMIRK TDAFGDMKDD HGDGSTSQPR NELVDPDYHA GGYVSTISDG
     TGTQLGGYTI ANGVEIENAT GGSGNDMLIG NNADNELVGN DGDDMLAGGA GDDTLTGGDG
     DDELIGGAGN DSLDGGEGHD IAYFSGPCSA YTIDRDDDDV VTISHLDGTG SEGVNTLVGV
     EEAKFSDATI DLLGEEDPEC PPLDFIFLVD LSSSFGNDLD NFVASAKQIA ADLRDENPDV
     QFSIASFIDK PESPWGGPED YLYKAHLEST SDVTEFESTL DGLSVRSGGD FPEAQWVGLY
     RAARGDGLDL REDSSRMIYM ATDASAHDAS DYGLDESNIQ AFLDGEDIDV EGDGTLSGSA
     SADEDGMDSL VEGDPDAVET EPDPRDPDDP GYDTGNEEPL PTDDLLLGAV GDALRDFGAV
     PIIGTSSSFT ESEYEEALAD MGSEGVVVST SSDSSDVADA VRAGRAAIEG EVTETGTSGD
     DSLVGTEDDD VILGLGGNDT IEGLGGNDTL DGGAGDDSLL GGDDDDALFG GTGADTIEGG
     AGDDVISPGA DADVITTGAG SDIITGPGDA LDGDTVTDMS ADDRVLVRFT RMRDEPTLDF
     DGTDTTLSFD TTGDGTQDFS MTFEGDVTDI GLLVSNAGEN VRIGTPPDMA LQVQDRGGNP
     LDVEEVTFRA DEGGPEWSGT PGGAAGAFSF TGLETAEGRI ETDLPYDPTE HGETPTSPGA
     LEALRLAVGL DPSWGPAAGE DFIAADFDGN GEVTSDDALD MLRLAVGLEA DDAPRWVFVN
     SDADMSGIDA GNVDVDAAAL AALPDFENDV SMTGILVGDM REFG
//
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