ID H6L378_SAPGL Unreviewed; 474 AA.
AC H6L378;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Gliding motility protein GldE {ECO:0000313|EMBL:AFC24905.1};
GN Name=gldE {ECO:0000313|EMBL:AFC24905.1};
GN OrderedLocusNames=SGRA_2176 {ECO:0000313|EMBL:AFC24905.1};
OS Saprospira grandis (strain Lewin).
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Saprospiraceae;
OC Saprospira.
OX NCBI_TaxID=984262 {ECO:0000313|EMBL:AFC24905.1, ECO:0000313|Proteomes:UP000007519};
RN [1] {ECO:0000313|EMBL:AFC24905.1, ECO:0000313|Proteomes:UP000007519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lewin {ECO:0000313|EMBL:AFC24905.1,
RC ECO:0000313|Proteomes:UP000007519};
RX PubMed=22675601; DOI=10.4056/sigs.2445005;
RA Saw J.H., Yuryev A., Kanbe M., Hou S., Young A.G., Aizawa S., Alam M.;
RT "Complete genome sequencing and analysis of Saprospira grandis str. Lewin,
RT a predatory marine bacterium.";
RL Stand. Genomic Sci. 6:84-93(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002831; AFC24905.1; -; Genomic_DNA.
DR AlphaFoldDB; H6L378; -.
DR STRING; 984262.SGRA_2176; -.
DR KEGG; sgn:SGRA_2176; -.
DR eggNOG; COG1253; Bacteria.
DR HOGENOM; CLU_015237_4_1_10; -.
DR Proteomes; UP000007519; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR002550; CNNM.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR044751; Ion_transp-like_CBS.
DR InterPro; IPR019862; Motility-assoc_prot_GldE.
DR InterPro; IPR005170; Transptr-assoc_dom.
DR NCBIfam; TIGR03520; GldE; 1.
DR PANTHER; PTHR22777; HEMOLYSIN-RELATED; 1.
DR PANTHER; PTHR22777:SF17; UPF0053 INNER MEMBRANE PROTEIN YFJD; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01595; CNNM; 1.
DR Pfam; PF03471; CorC_HlyC; 1.
DR SMART; SM00116; CBS; 2.
DR SMART; SM01091; CorC_HlyC; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS51846; CNNM; 1.
PE 4: Predicted;
KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW ProRule:PRU00703};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU01193}; Reference proteome {ECO:0000313|Proteomes:UP000007519};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU01193};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|PROSITE-
KW ProRule:PRU01193}.
FT TRANSMEM 39..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 39..233
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 252..311
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 316..373
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 474 AA; 53030 MW; D6CDD87715407779 CRC64;
MSSCSLGAAP LYSSSKRIIL DTDLIPSELG LSFLFLTDLG PATWISLGSI ILLLACSALL
SGSEVAFFSI THNDIEELQK QAVNKGGPRG RILRLLEKPH YLLSTILISN NFVNIGIILT
SNFLFAQLLP ESTPAWLSFL VTVVLVTFLL VLFGEVAPKV YATSNNMRLS KLMAQPLLLL
RRLFWPLSWV LVNATRIIER RLAKHSGMNV VTDKDIEQAI ELTVGDTKYA EQDIDILKGI
VKFGNTTVKN IMCARVDVEA VDSSINFSEL LAVLQNSNYS RIPVYEETFD KVLGIVHTKD
LIEHFDKDDS FDWHSLIRPA FFIPENKKID DLFNEFQHRR THMAIVVDEY GGSSGIVTLE
DVLEEIVGEI NDEFDEPESQ GYTKISEHIY IFEAKTSIQE ACKIMDIEPE LFEEARSSAE
TLAGLLLMIH GSMPKKNSQL LFQGIKFQVL STTKRRIETI KVTLAESAGE QVLA
//