ID   M4UH97_9XANT            Unreviewed;       900 AA.
AC   M4UH97;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Polysaccharide deacetylase {ECO:0000313|EMBL:AGH79780.1};
GN   ORFNames=XAC29_22005 {ECO:0000313|EMBL:AGH79780.1};
OS   Xanthomonas axonopodis Xac29-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=1304892 {ECO:0000313|EMBL:AGH79780.1, ECO:0000313|Proteomes:UP000011979};
RN   [1] {ECO:0000313|EMBL:AGH79780.1, ECO:0000313|Proteomes:UP000011979}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xac29-1 {ECO:0000313|EMBL:AGH79780.1,
RC   ECO:0000313|Proteomes:UP000011979};
RA   Chen G., Zou H., Ye G., Song X., Ji Z., Ma W.;
RT   "Completed genome of Xanthomonas axonopodis sp. Xac29-1.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP004399; AGH79780.1; -; Genomic_DNA.
DR   RefSeq; WP_011052927.1; NC_020800.1.
DR   AlphaFoldDB; M4UH97; -.
DR   GeneID; 66913342; -.
DR   KEGG; xao:XAC29_22005; -.
DR   PATRIC; fig|1304892.4.peg.4604; -.
DR   HOGENOM; CLU_324368_0_0_6; -.
DR   Proteomes; UP000011979; Chromosome.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd10917; CE4_NodB_like_6s_7s; 1.
DR   Gene3D; 3.40.50.1460; -; 1.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR029030; Caspase-like_dom_sf.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   InterPro; IPR011600; Pept_C14_caspase.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR46471; CHITIN DEACETYLASE; 1.
DR   PANTHER; PTHR46471:SF2; CHITIN DEACETYLASE-RELATED; 1.
DR   Pfam; PF00656; Peptidase_C14; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   Pfam; PF13424; TPR_12; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF52129; Caspase-like; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS51677; NODB; 1.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..900
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004059610"
FT   DOMAIN          257..447
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
FT   REPEAT          786..819
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          820..853
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          854..887
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ   SEQUENCE   900 AA;  97331 MW;  227A5FF6CAB0B341 CRC64;
     MTTSPLHRLL LCASCMGVLA LAGCGRHDAS DAAAAAKPAA ATSAGTQAGT AGDATPALIA
     QLRQQLDRHR RIIVLLADED KQRPRDRATS SSVGQQLFHE NLEQRERIAA SFDTVLISQD
     ARRFATIAAV LDEVESAPDL FDADRLAFAE VLRDLHARIG RDSALPAVKL HQRIGEDLEA
     LDEIERSYNK ELTQIFSRFD RSRAIVPKRE KWDDYVAHLR TLYTRENILR DHGVVEPYPF
     AARDSDSEVF GRDLPPKTVV LTFDDGPHRA YTEEIVAILK RYDVPGVFFE VGRNLGSLDA
     QGKAKLAPLS KISHTLMEEG YAVGNHSLTH AQLSKTTGDA LRSQVLDADA LLRAVDDKRA
     PLFRFPYGAR NAEGLQLLGE AGLKSIMWNI DSLDWADPVP ESIVQRVLDQ VNKEQRGIVL
     FHDIHDRAVK ALPQILDRLI ADGYQFAGWN GREFSVAHAP SALADATVTT GYAKSWAIVI
     GIDDYAQWPR LEYAANDAQA IASTLTGPLG FPSSQVIVLK NGQATRNNIL AAFHDRLGEG
     RAQTNDRVFV FFAGHGATRR LASGRDLGYI IPVDSDPQHL ASDAIAMSDL QNIAESLQAK
     HVLFVMDACY SGLGLTRGGP TSGAYLRENA RRIARQMLTA GGADQQVADS GPNGHSVFTW
     VLLQALAGKG DLNGDGLITG TELAAYVAPA VSAVSAQTPA FGSLPGSQGG EFVFQVPSGD
     EFLTAETAQL SADAIALNGR VDAARPASAA AGATVAAAPV TVKTLQGGQA TLVLPAAVKS
     SDRQRAQLAN ERGLQLYKEK RYVDAAEQFA EALKLRPDFA LAANNLGFVY YRQGRFAESA
     RWLENTLKID PSRAVAYLNL GDAYAKAGDR DKARKAYSTY LELQPQGSGA EQARTQLQSL
//