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Database: UniProt
Entry: A0A1Y2KB09_9PROT
LinkDB: A0A1Y2KB09_9PROT
Original site: A0A1Y2KB09_9PROT 
ID   A0A1Y2KB09_9PROT        Unreviewed;      1048 AA.
AC   A0A1Y2KB09;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Putative Heparinase II/III family protein {ECO:0000313|EMBL:OSM07114.1};
GN   ORFNames=MAIT1_03974 {ECO:0000313|EMBL:OSM07114.1};
OS   Magnetofaba australis IT-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales;
OC   Magnetococcaceae; Magnetofaba.
OX   NCBI_TaxID=1434232 {ECO:0000313|EMBL:OSM07114.1, ECO:0000313|Proteomes:UP000194003};
RN   [1] {ECO:0000313|EMBL:OSM07114.1, ECO:0000313|Proteomes:UP000194003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IT-1 {ECO:0000313|EMBL:OSM07114.1,
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: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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:OSM07114.1}.
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DR   EMBL; LVJN01000015; OSM07114.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2KB09; -.
DR   STRING; 1434232.MAIT1_03974; -.
DR   Proteomes; UP000194003; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   CDD; cd03801; GT4_PimA-like; 1.
DR   Gene3D; 2.70.98.70; -; 1.
DR   Gene3D; 1.50.10.100; Chondroitin AC/alginate lyase; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR008929; Chondroitin_lyas.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR012480; Hepar_II_III.
DR   InterPro; IPR031680; Hepar_II_III_N.
DR   PANTHER; PTHR39210; HEPARIN-SULFATE LYASE; 1.
DR   PANTHER; PTHR39210:SF1; HEPARIN-SULFATE LYASE; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   Pfam; PF07940; Hepar_II_III; 1.
DR   Pfam; PF16889; Hepar_II_III_N; 1.
DR   SUPFAM; SSF48230; Chondroitin AC/alginate lyase; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194003};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          181..342
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
FT   DOMAIN          501..720
FT                   /note="Heparin-sulfate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16889"
FT   REGION          455..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..496
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1048 AA;  115482 MW;  541F19696E5BE2A1 CRC64;
     MLILAPAGGN PHVLVGKPGG VGLYTRNLLR RMEPGVEMVH FVTGKRPGDP GWLWPLRLLG
     DAIRLKWTLF FQRFDIIHLN PSLNPKSTLR DALFLATIIG MRWWRRPRVL VFFRGWEWST
     ADAIQRSGWK RRGFRFLFGA ADHILVLAST FRQRLEQLGF DGARIELAAT MFDGDLIPTE
     PAPPHDEIGV LFLSSMNRNK GVTELLEGFA QVAAELPQLR LTLAGEGSAR AGAQTWVAAQ
     GLGDVVSLPG YVSGAAKGAL LQQADIFALP SRHGEGCPNA LLEAMGAGCA VIASRAGGIP
     DVITSDEHGE LLPEVSAAAV ADALRKLAGD SERLARCQAH NRETAWARYE SRQAAREMAQ
     RYRRMLIAPA SATGGGKLRW YAARLRAMSL GEIAYRAQRA VQKRLERRGW LTLPQPPAPT
     IVPATTWLKI PENEDPTVYT AAADAILAGT IPLFDEPTPG LGQPPNFNAD PATGDEPFAA
     GGADRKHSHS NPEKSRAKRR IWELNRHLHW VTLAQAWRVS GDKRYRDALL EQMRAWLDQC
     PYRTGPNWTS PLEMGVRLIN WALVWQILGG PHADCFQGGL GQELRDRLLA AVMQQAHYIQ
     RHLSRHTSAN NHLIGELAGL YVASRAWPYW PALARWGEDA KWELNEQIHL QVHVDGVGCE
     QTLDYQGFIA EFFLIAALVG ARTDDAFNAA YSSRMERMLA FLHAMLDAGG HLPQIGDADN
     GRAFCLNPAR DPAPQALLRL GAVCFARADF QAQAGALDVQ SRWLMGAHGR DRWAALARTP
     KAPRKQAFPQ GGYYILGQEF ETADEVHACV DCGPLGYLAI AAHGHADALA LTLSLGGVPI
     LVDPGTYDYH AGKQWRSHFR STAAHNTVSI DGADQSTQSG PFLWLNHAQS ACEAWEPEAA
     DDLFVGVCHG YERLPDPLTH RREARLFKAE SRLTTQDELI CRAPHEATRT WQFAAGAAVT
     QSGPQEVEAV VGPWRVTLRA DEADARLEII TGREEPPAGW VSDRYGRKQA APCVRFINTV
     AAATTLKCEI RWRRDADTEE YQGSKSHA
//
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