ID A0A1Q7A4B2_9CHLR Unreviewed; 338 AA.
AC A0A1Q7A4B2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=NodB homology domain-containing protein {ECO:0000259|PROSITE:PS51677};
GN ORFNames=AUI01_05610 {ECO:0000313|EMBL:OLB56949.1};
OS Ktedonobacter sp. 13_2_20CM_2_56_8.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Ktedonobacteraceae; Ktedonobacter.
OX NCBI_TaxID=1805232 {ECO:0000313|EMBL:OLB56949.1, ECO:0000313|Proteomes:UP000186629};
RN [1] {ECO:0000313|EMBL:OLB56949.1, ECO:0000313|Proteomes:UP000186629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLB56949.1}.
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DR EMBL; MNDS01000093; OLB56949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7A4B2; -.
DR Proteomes; UP000186629; 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; cd10917; CE4_NodB_like_6s_7s; 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; PTHR10587:SF105; CHITIN DEACETYLASE 1-RELATED; 1.
DR PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 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};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 24..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 121..301
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT REGION 64..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 338 AA; 36494 MW; 3A7954C4467DAAD4 CRC64;
MGLENIDGEV YFPRRAGAKI SRTSLVITLC AILGLLGSLM LTMTENYNSV QQSATAITAN
TPELATTSTT SPTNKATPAA PKSSPMNLQS PILPFPTLLW EQIAALQSHN RFLYTGNRYL
REIALTFDDG PNPYYTPQVL AVLQRYGVKA SFFCIGRQVA SYPDLVKQEY ADGNLVGNHS
WSHPNLALLS SDEIDSQINL TSNAIQQVIG VRPTLFRPPY GVVNARVLSK ANLLGLTTII
WSDEARDWTT PGTSVIVSRI LSLAGDGAII LMHDGGGDRS QTVAGLPTII TTLRLRGYQF
VTLQQMLKDL PKRPASTQAP IFVPTTIPSA SPAASPGP
//
