ID   A0A345QGT1_9RHOB        Unreviewed;       654 AA.
AC   A0A345QGT1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Tail length tape measure protein {ECO:0000313|EMBL:AXI44518.1};
GN   ORFNames=C1J02_19370 {ECO:0000313|EMBL:AXI44518.1};
OS   Sulfitobacter sp. SK011.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Sulfitobacter.
OX   NCBI_TaxID=1389004 {ECO:0000313|EMBL:AXI44518.1, ECO:0000313|Proteomes:UP000253968};
RN   [1] {ECO:0000313|EMBL:AXI44518.1, ECO:0000313|Proteomes:UP000253968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK011 {ECO:0000313|EMBL:AXI44518.1,
RC   ECO:0000313|Proteomes:UP000253968};
RA   Pohlner M., Engelen B., Bunk B.;
RT   "Comparative analysis of Sulfitobacter strains from the North Sea.";
RL   Submitted (JAN-2018) 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}.
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DR   EMBL; CP025803; AXI44518.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A345QGT1; -.
DR   OrthoDB; 9815002at2; -.
DR   Proteomes; UP000253968; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0008933; F:lytic transglycosylase activity; IEA:InterPro.
DR   GO; GO:0000270; P:peptidoglycan metabolic process; 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; IPR000189; Transglyc_AS.
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.
DR   PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000253968};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..654
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016940292"
FT   DOMAIN          488..591
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF01464"
SQ   SEQUENCE   654 AA;  72010 MW;  38C2B21604A4330E CRC64;
     MTRITATIAL VFALALPANA ERPRPLGWAM EAMRAGNWDT AALIANRDGP VAADVIEWHR
     LRAGRGTYAE ARAFLDRRPD WPGEAYLRKQ VEDDVIQQDD PAVLAFFAEM PPQTPSGVLA
     HAAALIRANQ RGEAEADVVL AWRTMPMNAT SQALFLAEHE GVLKPHHQAR LDEMLWQREH
     AEARQMFDLV GKDDVALAKT RIALQRREGD VNRLINALPA SKAGDPGLAH DRFEWRIRKN
     LAADAKTLLL EKSTSAEALG QPGKWSNRRR ALARDEMRSG NKKRAYQISS QHFLEPGSDY
     ADLEWLSGYI ALRFLDDPKA AYQHFLNHDS AVESPISQGR AGYWQGRALE ALGDADGAAK
     AYAMGAQFQT SFYGLLAAER AGLPFDMTLA GETPAQNWRS SPLASAPLFE AGMLLQASGE
     LSVAERFWSH LADQLVSDDL ALLGQAAIDT DQPHLAVMIG KRAARRGLTI AAPYYPMHSL
     VELDLPMAPE MTLAIARRES EFDPVVQSAV GARGLMQIMP ATAREVAADL AITALHTTDR
     LTADPDYNAR LGAKYLSQMA GRFDGNVSMM AAAYNAGPSR PIRWMADYGD PRKGKIDIVD
     WVEMIPFRET QNYVMRVTES LPVYRARLGK DPLPVPFSKE LVGSTLKGFA PKGE
//