ID K9PH67_9CYAN Unreviewed; 731 AA.
AC K9PH67;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Lytic transglycosylase catalytic {ECO:0000313|EMBL:AFY32291.1};
DE Flags: Precursor;
GN ORFNames=Cal7507_1837 {ECO:0000313|EMBL:AFY32291.1};
OS Calothrix sp. PCC 7507.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=99598 {ECO:0000313|EMBL:AFY32291.1, ECO:0000313|Proteomes:UP000010390};
RN [1] {ECO:0000313|EMBL:AFY32291.1, ECO:0000313|Proteomes:UP000010390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7507 {ECO:0000313|EMBL:AFY32291.1,
RC ECO:0000313|Proteomes:UP000010390};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Teshima H., Chen A.,
RA Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L., Pitluck S.,
RA Woyke T., Kerfeld C.;
RT "Finished genome of Calothrix sp. PCC 7507.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000256|ARBA:ARBA00007734}.
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DR EMBL; CP003943; AFY32291.1; -; Genomic_DNA.
DR RefSeq; WP_015128107.1; NC_019682.1.
DR AlphaFoldDB; K9PH67; -.
DR STRING; 99598.Cal7507_1837; -.
DR KEGG; calo:Cal7507_1837; -.
DR PATRIC; fig|99598.3.peg.2060; -.
DR eggNOG; COG0741; Bacteria.
DR eggNOG; COG1729; Bacteria.
DR HOGENOM; CLU_013746_0_0_3; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000010390; 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; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR008939; Lytic_TGlycosylase_superhlx_U.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
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 Pfam; PF13174; TPR_6; 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:UP000010390};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 569..682
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
SQ SEQUENCE 731 AA; 82506 MW; 256ED02C9BE82EA9 CRC64;
MLKQLKKNPI PIIAGAGLFA FLAGAMVSAP QIGKSLGQWL KHGNNQPEQI SEATKAKSAV
YPLVSQSLPE RAAKLAAIAQ DSRSPDQKRA RYLLASDYIE RTQAQKALIL LTGLEKDYPI
LAPYILLKQA QAEDMLGEEG KASDLRQQVL KQYPKTAAVV KAIYLIAQPQ LQDQAIAQFP
SHPLTWEIIR KRLQDNPNQP QLQLILAKYA TDQPGIVGVL DDLVKQPNLK SEDWEIIGAA
YWANSEFDKA AKAYAKAPKT AENLYRNGRG LQVGGKEQEK AIAIYKQVVQ QFPESTETGT
ALLRLAELAK TRKDALPYLD QIIKSFPDIA GKALVEKAKI FQGLKDTKSA SETWQLLIAK
YGNSDEAAEY RWKIAQEKAK AKDYLGAWQW AEPITTNNPN SILAPRAGFW VGKWATSLGK
QQEAKTAYEY VLSQFPYSYY AWRSASILGL NVGNFNTIRQ MNPEVVPFQR PVPTAGSETF
KELYLLGQNR DAWLQWETEF QNKTKPTVAE QFTEGLMRLA NGENLIGIDK ISKLEDREIP
AEQAQYQALS KQSIYWQARY PFPYFQEIVK WSNERKLNPL LVTALMRQES RFEAKIKSSA
NATGLMQIIP DTAKWIAPQI KLDSKQINLE NPNDNIMLGT WYLDHTHQKY NNNSLLAIAS
YNAGPGNVSK WLQTISTKDS DEFVEEIPFD ETKNYVRQVL GNYWNYLRLY NPEISNIVGQ
YSAQHPQLPT Q
//
