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Database: UniProt
Entry: A0A8G2CKC4_ACIRU
LinkDB: A0A8G2CKC4_ACIRU
Original site: A0A8G2CKC4_ACIRU 
ID   A0A8G2CKC4_ACIRU        Unreviewed;       619 AA.
AC   A0A8G2CKC4;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 12.
DE   SubName: Full=Transglycosylase SLT domain-containing protein {ECO:0000313|EMBL:SIQ73010.1};
GN   ORFNames=SAMN05421828_108125 {ECO:0000313|EMBL:SIQ73010.1};
OS   Acidiphilium rubrum.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Acetobacterales; Acidocellaceae; Acidiphilium.
OX   NCBI_TaxID=526 {ECO:0000313|EMBL:SIQ73010.1, ECO:0000313|Proteomes:UP000186308};
RN   [1] {ECO:0000313|EMBL:SIQ73010.1, ECO:0000313|Proteomes:UP000186308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35905 {ECO:0000313|EMBL:SIQ73010.1,
RC   ECO:0000313|Proteomes:UP000186308};
RA   Varghese N., Submissions S.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:SIQ73010.1}.
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DR   EMBL; FTNE01000008; SIQ73010.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A8G2CKC4; -.
DR   OrthoDB; 9815002at2; -.
DR   Proteomes; UP000186308; Unassembled WGS sequence.
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; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE C; 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:UP000186308};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..619
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5034808944"
FT   DOMAIN          453..550
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF01464"
FT   REGION          33..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   619 AA;  64488 MW;  25FF828B80BDEE3B CRC64;
     MRGAVKKLSR LSVARACIVS AALLATVAPA SAAPAGQRGS TTAKHAGVSQ PATEPLGSSG
     SESVAYAIPR STPLNGAETM LAQPLTPSDA ATYQRIFADQ HQGKMAAAQR LLDRVDNPLL
     KGQVLAQRYL GPYHHATPAE LQAWLAAYNG QPHTLRIRAL LLQRLPRGAS APTAAVTYLP
     EPIMAASGAA PPPPPGVPVP RYLADRVANL TRAGHTSLAI DLIGRDNHIS TAAGAALRGD
     VARNLFINAR YAEAFTVASQ AAHEGGDAVW RPDFIAGLAA WQLHKIAEAL PYFTAAASAT
     HTSPGERAAG AFWAARAALR LRHPDAYLHW LDQAAAAPDS FYGMLAGRLL GHGLDGTGLS
     ASLSEADIEA VAAHKNGALA FALIEVGRPA DAARALRALW PDIRREAGFG RAVMRVAARA
     GLVDVAVALD QRLPGNAIAG TSLPLPALHP AGGFNVDPSL IYALARTESG FNVNAVSPVG
     ARGLMQLMPQ TAAAMARIGG IGGNMSAPAV NLALGQSYLR YLGKQPGVQR NLLDILASYN
     AGPVAAAAWA HSIHDGGDPL IFLESIPLAQ TRRFVRQVLA DSWLYAEQLG TTPESLDAMA
     EGKFPRLSPY GTALADAGD
//
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