ID A0A1I6L8L7_9BACT Unreviewed; 1022 AA.
AC A0A1I6L8L7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Component of the Tol biopolymer transport system {ECO:0000313|EMBL:SFR99819.1};
GN ORFNames=SAMN05421771_0420 {ECO:0000313|EMBL:SFR99819.1};
OS Granulicella pectinivorans.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Granulicella.
OX NCBI_TaxID=474950 {ECO:0000313|EMBL:SFR99819.1, ECO:0000313|Proteomes:UP000199024};
RN [1] {ECO:0000313|EMBL:SFR99819.1, ECO:0000313|Proteomes:UP000199024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21001 {ECO:0000313|EMBL:SFR99819.1,
RC ECO:0000313|Proteomes:UP000199024};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TolB family.
CC {ECO:0000256|ARBA:ARBA00009820}.
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DR EMBL; FOZL01000001; SFR99819.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6L8L7; -.
DR STRING; 474950.SAMN05421771_0420; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000199024; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 3.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR011659; PD40.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
DR PANTHER; PTHR36842; PROTEIN TOLB HOMOLOG; 1.
DR PANTHER; PTHR36842:SF1; TOL-PAL SYSTEM PROTEIN TOLB; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF07676; PD40; 8.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR SUPFAM; SSF69304; Tricorn protease N-terminal domain; 1.
DR SUPFAM; SSF50969; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000199024};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1022
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011711200"
FT DOMAIN 693..997
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 1022 AA; 109513 MW; 0DD0297DFB60506E CRC64;
MRFASVLPLA LSSVALMAAP PTPAVTPHKV ITVHEGTNMA VTVSPDHRTI LMDLQGMIYA
IPFAGGAAKR VTGPLVEASH PEYSPDGKWV AIQSYAGGTF HIWVMRPDGT GLKQMTTGHG
DDREPRFSPD GKTIAFSSDR ANKGSYDIWT VDVASGAVKQ ITSSENDEYE PAWSPDGSSL
AYVNGVFVAG APGVGGVVGR TVESVDLATG ATKTVASIGR QVGRIESPSW SPDGKHLAYI
QFMGAGMFVD AARLVVDGKP VAGGGVKDDD AFPFPPVWLS DASILYTANG AILKVDLGAG
TKTAIPFTAG IESIRPVYKG KDFGFNATAT RQALGLFSPA LSPDGKKAAF VALNQLYLLT
VGNPVPKALT HDTYYKQGPA WSPDGKTLAY VSDKDGVENI YLMDVATGTD KRAAASMDAQ
IFPAWSPDGR WMAFQKQDGA TMLLELSSGA ISPLAPATFF PGRPAFSPDG KTVAIATVKP
YSKRFREGTS SILTVDLATK KTTWYDPAPF ESITTRTEDG PVYSPKGEIA FIMDDLLYAM
PVDAMGKPDG AAVALNGETS DAPTYNGDGS KILYVSNGKL RLLDRKTKAI TPVPVTLTYK
PLQPKPTDKV LIHAGKFWKG EGAETLTDVD VLVVGNRVAS VKPHGGPVPA GAMVIEAPHS
TLLPGLWENH AHPNSDNSIY YGDRMGRLWM VYGITTLRDM ADQAYRAVEE KESFVSGAAV
GPRLFATGEA IDGERTYYPM MIPTTSEAQL HREFERLHAL DFDFMKLYVR LPYTWIVEGV
KYAHGTMGVQ TAGHYLLPAV DLGNDGMSHV SATARTGYAY SRSLTGASYS DVRQLMAESG
MWTTSTLLNQ GVIAQMPEMA DDTRYNLAPP WEKKRLIAAR DAAMKSDQTA NEDRVMKEEA
TLRGVLERKG MYIGGTDSPL DLPSTSLHLN ILSQVKFGLA PWQALETVTS TAARAAKVDK
DLGLIAPGYL ADMILVEGDP LVNIKDVTKV QCVMKNGAIH SVGELMAPFV KSDVGVGMCP
AK
//
