ID J3BBP6_9PSED Unreviewed; 1350 AA.
AC J3BBP6;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Parallel beta-helix repeat (Two copies) {ECO:0000313|EMBL:EJM82018.1};
GN ORFNames=PMI34_04938 {ECO:0000313|EMBL:EJM82018.1};
OS Pseudomonas sp. GM74.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144336 {ECO:0000313|EMBL:EJM82018.1, ECO:0000313|Proteomes:UP000007290};
RN [1] {ECO:0000313|EMBL:EJM82018.1, ECO:0000313|Proteomes:UP000007290}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM74 {ECO:0000313|EMBL:EJM82018.1,
RC ECO:0000313|Proteomes:UP000007290};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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:EJM82018.1}.
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DR EMBL; AKJG01000153; EJM82018.1; -; Genomic_DNA.
DR RefSeq; WP_008053417.1; NZ_AKJG01000153.1.
DR PATRIC; fig|1144336.3.peg.4818; -.
DR Proteomes; UP000007290; 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:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProt.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 5.
DR Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR006633; Carb-bd_sugar_hydrolysis-dom.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR022441; Para_beta_helix_rpt-2.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR024535; Pectate_lyase_SF_prot.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR013858; Peptidase_M10B_C.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR NCBIfam; TIGR03804; para_beta_helix; 1.
DR PANTHER; PTHR38340; S-LAYER PROTEIN; 1.
DR PANTHER; PTHR38340:SF1; S-LAYER PROTEIN; 1.
DR Pfam; PF00353; HemolysinCabind; 6.
DR Pfam; PF12708; Pectate_lyase_3; 1.
DR Pfam; PF08548; Peptidase_M10_C; 1.
DR PRINTS; PR00313; CABNDNGRPT.
DR SMART; SM00722; CASH; 2.
DR SMART; SM00710; PbH1; 10.
DR SUPFAM; SSF51120; beta-Roll; 5.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR SUPFAM; SSF52266; SGNH hydrolase; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 6.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 9..201
FT /note="Carbohydrate-binding/sugar hydrolysis"
FT /evidence="ECO:0000259|SMART:SM00722"
FT DOMAIN 216..359
FT /note="Carbohydrate-binding/sugar hydrolysis"
FT /evidence="ECO:0000259|SMART:SM00722"
SQ SEQUENCE 1350 AA; 139973 MW; 72F4C0EB982EAADD CRC64;
MIFNVQNFGA KGDGITDDTA AIQNAIDAAA AAGGGQVYMP TGTYIVSGGE EPSDGCLMLK
SNVYLYGDGM GATTVKVADG SDTKITGVIR SAYGEQTHDF GVSNLTIDGN RDNTTGKIDG
WFNGYIPGEA GFDSNVTLDS VEIKDCSGYG FDPHEQTVNM VIKNSVSHGN GLDGFVADFL
SDSTFENNVA YDNDRHGFNI VTSTHDFTLT NNVAYNNGGT GIVVQRGSED IPSPSNITIT
GGEVYGNGAE GVLIKLSSEV TVSGVDIHDN ASTGVRIYGS NHVEIIDNTL NNNSLGSPVP
EIIIQSYDDT LGVSGKYFNG SDNIIQGNII SGSNLSTYGV AERNEDGTDR NAIIGNTISH
TSNGATLIYG DGSYVSATVP MTIVQGTDGN DTLPGSAASE IFYGGAGNDT INGGAGGDIL
AGGAGIDKLT GGTGADTFRF TAQSESYRNA TTSFDDSITD FDVTQDKIDL ADLGFTGLGN
GRGGTLQVSY SASSDRTYIK DFDADASGNR FELILSGNLA GTLTASHFIF NRVITGTSAS
DSLLGSDSGD TLLGLAGNDS LSGGAGDDKL DGGAGRDSLY GGDGADTFRY SNVLDSYRDY
DTGGVTATDT IYDFTAGVDK IDVSSLGFLG LGDGSNGTLY LTLNSAGDKT YIKSAEADAD
GNRFEIALNG NYLDTLTASD FVFGEPARQD ILYLPTLGQS NARLLRMTED DAQSGTSMLV
NDLDRYTPYD VRSQFTDANG NGIDIAVGGS TVTGLSTLSA GELELCWWLT DTNQPGAALL
RAVTLLRDQI SELQSISNVT MGIIWGQGEE AAQEVARATD KAAAAAAYKA ATLKVFDYLH
AQFGNFSVYM METGHYDQDA ARARGYSQEK IASIVEGAGY VRAAQEAIAA ERADVKLAVD
YTDLPLRHEV DPLTYPDDVW HLHEESAEIV GQRLADYIAG DLGLQGNPND NNSVQDIFDN
ARNLISGTAQ ADTLVGSSDN DTLDGDLGAD TMTGGNGNDI YVVDNASDRV VETSTSTSQI
DTVQASVSWT LGANLENLVL TGVSDINGTG NERHNFITGN AANNLLDGAA GADSMSGGDD
NDTYYVDNAD DAVIEINGNA ASGGVDSVHS SVAAFTLGNN VEHLYIDSTG AANGTGNALD
NTLFAGPGNN VLDGRDGIDT VSFERALSGV TVNLSTSAQQ NTTGSGLDTL RSCENLTGSA
YADSLSGNSA ANILNGGAGN DTLVGGSGND RLIGGAGTDN LTGGTGADTF AFSALSDMGV
GALRDVINGF KSIEGDHLDF TGLDARPLTT AVDAFTFIGS NAFDPANATG QLRFADGVLQ
GSVNADATPE FEIQLVGVQQ LNASDFTALG
//