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Database: UniProt
Entry: Q4L5L2_STAHJ
LinkDB: Q4L5L2_STAHJ
Original site: Q4L5L2_STAHJ 
ID   Q4L5L2_STAHJ            Unreviewed;       603 AA.
AC   Q4L5L2;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   24-JAN-2024, entry version 102.
DE   RecName: Full=NodB homology domain-containing protein {ECO:0000259|Pfam:PF01522};
GN   OrderedLocusNames=SH1754 {ECO:0000313|EMBL:BAE05063.1};
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808 {ECO:0000313|EMBL:BAE05063.1, ECO:0000313|Proteomes:UP000000543};
RN   [1] {ECO:0000313|EMBL:BAE05063.1, ECO:0000313|Proteomes:UP000000543}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435 {ECO:0000313|EMBL:BAE05063.1,
RC   ECO:0000313|Proteomes:UP000000543};
RX   PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
CC   -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC       {ECO:0000256|ARBA:ARBA00010973}.
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DR   EMBL; AP006716; BAE05063.1; -; Genomic_DNA.
DR   RefSeq; WP_011276037.1; NC_007168.1.
DR   AlphaFoldDB; Q4L5L2; -.
DR   KEGG; sha:SH1754; -.
DR   eggNOG; COG0726; Bacteria.
DR   HOGENOM; CLU_452622_0_0_9; -.
DR   OrthoDB; 9778320at2; -.
DR   Proteomes; UP000000543; Chromosome.
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; cd10970; CE4_DAC_u1_6s; 1.
DR   CDD; cd19958; pyocin_knob; 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:SF3; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE N-DEACETYLASE; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          111..224
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|Pfam:PF01522"
FT   COILED          46..73
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   603 AA;  68887 MW;  33C0CD369CA54BA5 CRC64;
     MTRKIITSIW DRVNLLSIND NFTELYEEIR TIIASQLDAE FVLEEARRVN RENTETKIGI
     QKLKNELDQL VIESGNPNAE VSMARGLSKT LGEEIERIDN KTYTKDSNKV RPLVSFYLDD
     GYQNDYDVVF PKAKSLGIPV TACLFNTSEL LSTPERLKEL IDNGWEIHSH TAHHVDLDKM
     SLDEQMKEMR DNILYYKDLG IDLKGICYPK GYSNEYTPKA ARQYFEVGMS SIPGINSTPI
     DTYYVYRDLT DQTDMSIMKK RVDTILEEGK GWLVFYSHTN IFKQNTMVRD RYFEMMDYVK
     SKGIECVTVH DAMKVYGNTL DIGDVKYSEN YLKVGSDGVL DTSNLPIIYN KNLTNVSSIK
     GTDFKDGKIT ITSFDLSKKS DIPFDSGVGT LYTDRRFELN KYGQRAFQRF EGIDGTIVQR
     VYNAGNWSDW SSAGVLNSVK KAYNNASPIT EFPKFKKSIN TFISSDNSGL PEPIGTLETT
     RISANDVLNY QIFYPYNKNI FYKRYWTSNG WADWSKFTNS IFYTQSYDFG DIEANATRTY
     SFTINGVNDN DVPTINFVQG LINGLVPYIY TAGNNTVVVK LLNVYNTKIT IGTRPIRIAV
     NKN
//
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