ID S6GYP2_9PSED Unreviewed; 1609 AA.
AC S6GYP2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Poly(Beta-D-mannuronate) C5 epimerase 3 (Mannuronanepimerase 3) {ECO:0000313|EMBL:EPJ79687.1};
GN ORFNames=CFII64_20763 {ECO:0000313|EMBL:EPJ79687.1};
OS Pseudomonas sp. CFII64.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=911242 {ECO:0000313|EMBL:EPJ79687.1, ECO:0000313|Proteomes:UP000014850};
RN [1] {ECO:0000313|EMBL:EPJ79687.1, ECO:0000313|Proteomes:UP000014850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFII64 {ECO:0000313|EMBL:EPJ79687.1,
RC ECO:0000313|Proteomes:UP000014850};
RA Feris K.P., Lalor S.J.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:EPJ79687.1}.
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DR EMBL; ATLO01000043; EPJ79687.1; -; Genomic_DNA.
DR PATRIC; fig|911242.4.peg.4132; -.
DR OrthoDB; 7329412at2; -.
DR Proteomes; UP000014850; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0016020; C:membrane; 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; 4.
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; IPR006644; Cadg.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR006633; Carb-bd_sugar_hydrolysis-dom.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
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 InterPro; IPR019960; T1SS_VCA0849.
DR NCBIfam; TIGR03661; T1SS_VCA0849; 1.
DR PANTHER; PTHR38340; S-LAYER PROTEIN; 1.
DR PANTHER; PTHR38340:SF1; S-LAYER PROTEIN; 1.
DR Pfam; PF05345; He_PIG; 1.
DR Pfam; PF00353; HemolysinCabind; 7.
DR Pfam; PF12708; Pectate_lyase_3; 1.
DR Pfam; PF08548; Peptidase_M10_C; 3.
DR PRINTS; PR00313; CABNDNGRPT.
DR SMART; SM00736; CADG; 1.
DR SMART; SM00722; CASH; 2.
DR SMART; SM00710; PbH1; 9.
DR SUPFAM; SSF51120; beta-Roll; 6.
DR SUPFAM; SSF49313; Cadherin-like; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR SUPFAM; SSF52266; SGNH hydrolase; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 8.
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..399
FT /note="Carbohydrate-binding/sugar hydrolysis"
FT /evidence="ECO:0000259|SMART:SM00722"
FT DOMAIN 694..792
FT /note="Dystroglycan-type cadherin-like"
FT /evidence="ECO:0000259|SMART:SM00736"
FT REGION 1207..1235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1609 AA; 166168 MW; 9D5043E245C21870 CRC64;
MIFNVKNYGA LGDGITDDTA AIQAAIDAAA AAGGGTVEMS AGTYIVSAGE EPSDGCLMLK
SNVTLSGAGM GETVIKLQDG SDTKVTGIVR SAYGEETHDF GMNNLTLDGN RDATTGKVDG
WFNGYIPGSA GKDSNVTLDS VEIVDCSGYG FDPHEQTVNM VIKNSVSHGN GLDGFVADFL
SDSVFENNIA YNNDRHGFNV VTSTHDFTLT NNVAYGNGST GIVVQRGSEN IPSPANITIT
GGEIYGNGAE GVLIKLSSEV TVSGVNIHDN TSAGIRIYGS SNVDVVDNTL TNNSLGAPVP
EVIIQSYDDT QGVSGKYFDG SDNLIRGNTI TGSDKSTYGV AERDEKGTDG NSIVGNTISH
TSKGLVLIYG DGSYVGDALP VVAVQGTTGN DTISGSAANE LLFGLAGKDT LNGNAGDDIL
VGGNGADKLT GGAGADTFRF DLVTDSYRTA TASFADLITD FDISQDKIDL ANLGFSGLGS
GTAGTLNISY NASLDRTYVK SLTADAEGNR FELGLSGNLL GKLDASHFIF QRVIEGTAAN
DTLVGTDGID TLNGNGGADR IDGGAGADRI NGGADADTLT GGAGADTFVY SSRMDSYRNY
NTSTSKQSDT ITDFNVSQDR IDLSAVGLRG LGDGSNNTVY LSLNADGSKT YVKTNAIDDT
GNRFEIALQG NLLSSLSADN FIFSSASTVN QAPVLNTPLL DQATNTQTAF SYTVQANSFS
DPDKDALTYS ATLADNTALP DWLKFDSKTL TFSGTPSVAS GTYSVLLTAS DAAGASVSDS
FAITVGNPTP GVITGSDKGE SLYGTTGNDV MQGLGGADTI RGDAGNDLIN GGAGRDALYG
GAGNDTFVYS AVSDSYRDYD SGGLTATDTI YDFTPGEDKI DVSALGFLGL GDGENHTLYM
TLNAAGDKTY VKSSVVDADG NRFEIALSGN LIDQISDADF VFAQRESQEI LYLPTLGQSN
ARLLRMTEDD DQSGTSTLVS DLARYTDYDV RSQFTDADGN GIDLAVGGST VAGYSTSTLE
EQRLSWWLTD TDQPGPALLR AVELLKTQLA TLTAIDTVTT GIIWGQGEEA AQEIARATDK
QAAADLYKAS TLKVFDYLHA QIGDFNVYLM ETGHYQTDAA AARGFSAEKI AGIVEGVGYV
RAAQEAMATE RSDVKLAVDY TDLPLRHEVD PLVYPDDVWH LHEESAEIVG QRLADYIATD
LGYTSDSSDN NSAADITEGT QNEGGSIFGT ADDDTLMGSR GNDTLDGDLG ADAMTGGDGN
DIYVVDNAGD SVTETNTSAS QIDAVLASVS WTLGANTENL TLTGMSAIDG VGNELKNIII
GNSASNILDG QAGADSLKGG DGSDSYFVDD ANDKVIETNA DSVTGGVDTV YSALTTYTLG
SNVENLLLTG AGAANGIGNA LDNVLYAGSG DNLIDGRAGI DTVSYLFATA GVTVKLSTTA
QQDTGGSGLD TLKGNENLTG SRFADSLTGS SADNRLAGGD GNDTLSGGSG NDVLIGGAGV
DTLIGGTGAD TYVFNDVSEM GSGLLADIIQ GFKSAEGDKL DFSAIDARPQ TAANDAFVFI
GSAAFSANNV GELRFADGVL YGNTDADNEA DFAIQLTGVQ TLQAADIIG
//
