ID   N1TXK4_9LEPT            Unreviewed;       536 AA.
AC   N1TXK4;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Polysaccharide deacetylase {ECO:0000313|EMBL:EMY13013.1};
GN   ORFNames=LEP1GSC043_4696 {ECO:0000313|EMBL:EMY13013.1};
OS   Leptospira weilii str. Ecochallenge.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1049986 {ECO:0000313|EMBL:EMY13013.1, ECO:0000313|Proteomes:UP000012249};
RN   [1] {ECO:0000313|EMBL:EMY13013.1, ECO:0000313|Proteomes:UP000012249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ecochallenge {ECO:0000313|EMBL:EMY13013.1,
RC   ECO:0000313|Proteomes:UP000012249};
RA   Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA   Sanka R., DePew J., Purushe J., Haake D.A., Matsunaga J., Vinetz J.M.,
RA   Sutton G.G., Nierman W.C., Fouts D.E.;
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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:EMY13013.1}.
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DR   EMBL; AHMI02000263; EMY13013.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1TXK4; -.
DR   Proteomes; UP000012249; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd10918; CE4_NodB_like_5s_6s; 1.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   PANTHER; PTHR34216; -; 1.
DR   PANTHER; PTHR34216:SF8; POLYSACCHARIDE DEACETYLASE-LIKE PROTEIN; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          275..536
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
FT   REGION          98..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..118
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..142
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..191
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   536 AA;  60763 MW;  414874C7F03214E3 CRC64;
     MQTKPFTVRF KTLISFHPKK QSYEGTQCFV CLHRVLPDRK TQETLQNTFY GSYFGHIPLL
     FRFLINNIMR NTLTTFAIFY LLISSILIAS PVNDFLNPEK KRKPTASSPK KDTEQKPSYT
     PEDFSQKAVS KKNQKEKTES ANVDSDTTQS EDKVSRKKST VKSQKGSDSK QENFEVSKNP
     KKKKYEDALP TVKEDTPPTP SYTIQGVESV SGGGIPVLCY HHLASEGGPM GGYNLHPNLL
     EEQFKFLKAT GYNTVRLDQF YAYINGKKPS DFPDKPILLT FDDGSKTHFE VLVPLLKKYG
     FTASIFIYPS IISSGKKYYM TWEELKRALD SGVLDLGSHT LYHPKLPTMS RAFIRKQLAE
     SKQILEAKTG RKVIDLAYPF GLFDPRVIEE AKAIGYRMAF TVNPGKNLPG TPIYNIHRSL
     VPWGQSQSAF NSILTMAPPP KISISIQDGS WVKTGQEFKI HLEGVQPESV SIKIKSKNVL
     LENQPPDYTV RIPSFAKKST FLPLMVQAKT KDGKQIQYQY LFINQKEFQK HPDGDF
//