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Database: UniProt
Entry: M9RFC1_9RHOB
LinkDB: M9RFC1_9RHOB
Original site: M9RFC1_9RHOB 
ID   M9RFC1_9RHOB            Unreviewed;       716 AA.
AC   M9RFC1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Transglycosylase-like protein {ECO:0000313|EMBL:AGI70433.1};
GN   ORFNames=OA238_c01640 {ECO:0000313|EMBL:AGI70433.1};
OS   Octadecabacter arcticus 238.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Octadecabacter.
OX   NCBI_TaxID=391616 {ECO:0000313|EMBL:AGI70433.1, ECO:0000313|Proteomes:UP000004688};
RN   [1] {ECO:0000313|EMBL:AGI70433.1, ECO:0000313|Proteomes:UP000004688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=238 {ECO:0000313|EMBL:AGI70433.1,
RC   ECO:0000313|Proteomes:UP000004688};
RX   PubMed=23671678;
RA   Vollmers J., Voget S., Dietrich S., Gollnow K., Smits M., Meyer K.,
RA   Brinkhoff T., Simon M., Daniel R.;
RT   "Poles Apart: Arctic and Antarctic Octadecabacter strains Share High Genome
RT   Plasticity and a New Type of Xanthorhodopsin.";
RL   PLoS ONE 8:E63422-E63422(2013).
CC   -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC       {ECO:0000256|ARBA:ARBA00007734}.
CC   -!- SIMILARITY: Belongs to the virb1 family.
CC       {ECO:0000256|ARBA:ARBA00009387}.
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DR   EMBL; CP003742; AGI70433.1; -; Genomic_DNA.
DR   AlphaFoldDB; M9RFC1; -.
DR   STRING; 391616.OA238_c01640; -.
DR   KEGG; oar:OA238_c01640; -.
DR   eggNOG; COG0457; Bacteria.
DR   eggNOG; COG0741; Bacteria.
DR   HOGENOM; CLU_015184_0_0_5; -.
DR   OrthoDB; 9815002at2; -.
DR   Proteomes; UP000004688; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   CDD; cd13401; Slt70-like; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 1.25.20.10; Bacterial muramidases; 1.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR008939; Lytic_TGlycosylase_superhlx_U.
DR   InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR   PANTHER; PTHR37423:SF2; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE; 1.
DR   PANTHER; PTHR37423; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE-RELATED; 1.
DR   Pfam; PF01464; SLT; 1.
DR   SUPFAM; SSF48435; Bacterial muramidases; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000004688};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..716
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004102485"
FT   DOMAIN          502..603
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF01464"
FT   REGION          687..716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   716 AA;  78733 MW;  9A7E1E8EFDA1771C CRC64;
     MGGQTILTIR TLCVAAILLA SPATAKNVSN SDATSPFSRA LTLLANGDAD GAYDSLADRS
     AVEQDLLEWM QLRDTGTDFT FSSYTAFLER RSEWPGNDAI RANAERVIDE TIPNDDVLTF
     FDGSGAETGQ GAVAYANALI ADGRRDAAEA MLVDLWLTSA FTTASHQAIV NAFADVVAPH
     HFARADMLLW RWRTSDVANV VPLLDAGQQA LIRARLANIN RDSDIEARED LIPDRLQDTP
     GLHYDRFNRF VDRGDWTQAS IILTAQSNSA ERLGIPWRWG SWRRILARWH MRKGNIDVAY
     RFATQHFIQP DEDNYSDLEW LAGYIALTHM KDYDAALVHF QRFDDSVSSP ISKGRAGYWL
     GRAHEGLGNA DAAITAFRMG AQHQTSFYGL LSAEKLGLTL SADIVGGEDF GDWRSIPMLN
     ADLVRAGLAL LDAGERGLAV LFFRDAAAGM TRQEIGQLGA LFMDLGDPFY TVLIAKTAVQ
     GDLLVQDAYF PVHPMADLDL PVEPALALAI ARQESEFRTD AGSSVGALGL MQLMPATAQE
     VAGWLDMPYS LSRLTTDWAY NTTLGSEYLA YLTREFGNSP VMIAASYNAG PSRPKSWITE
     RGDPRLSVLN PDPVDVIDWI EHIPFRETRN YVMRVTEGIP VYRARLTGQI GPVRFMDILV
     GEAPVIRPVA RPSRTVDAIL EAAPTQLRPP VRRAGEVEPV PPTGPQPTRP VARAND
//
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